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102 hits found for Peptide

SASDFE2 – ...Peptide (LAP)

Latency Associated Peptide experimental SAS data
Latency Associated Peptide Kratky plot
Sample: ...Peptide dimer, 58 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 4
Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses. J Synchrotron Radiat 26(Pt 4):967-979 (2019)
Stachowski T, Grant TD, Snell EH
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 179 nm3

SASDRS2 – ...peptide Mannan-binding lectin (MBL) center

Ac-(POG)4-QG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-QG-(POG)5-NH2 trimer, 11 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.1 nm
Dmax 8.7 nm
VolumePorod 7 nm3

SASDRT2 – ...peptide Mannan-binding Lectin (MBL) native

Ac-(POG)4-QG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-QG-(POG)5-NH2 trimer, 11 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 1.7 nm
Dmax 7.1 nm
VolumePorod 4 nm3

SASDRU2 – ...peptide Mannan-binding lectin (MBL) with EOG sequence

Ac-(POG)5-EOGQGLRG-(POG)3-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)5-EOGQGLRG-(POG)3-NH2 trimer, 12 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.3 nm
Dmax 10.0 nm
VolumePorod 6 nm3

SASDTU2 – NAD-dependent protein deacetylase sirtuin-7 at pH 8.0

Isoform 1 of NAD-dependent protein deacetylase sirtuin-7 experimental SAS data
CORAL model
Sample: Isoform 1 of NAD-dependent protein deacetylase sirtuin-7 monomer, 45 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Dec 16
...Peptide Inhibitors of the Oligonucleotide-Activated Sirtuin 7. Angew Chem Int Ed Engl :e202314597 (2023)
Bolding JE, Nielsen AL, Jensen I, Hansen TN, Ryberg LA, Jameson ST, Harris P, Peters GHJ, Denu JM, Rogers JM, Olsen CA
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 89 nm3

SASDRV2 – ...peptide Mannan-binding lectin (MBL) 12 triplets

Ac-(POG)5-EPGQGLRG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)5-EPGQGLRG-(POG)5-NH2 trimer, 14 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.8 nm
Dmax 12.5 nm
VolumePorod 16 nm3

SASDHZ2 – 14-3-3 protein beta isoform

14-3-3 protein beta/alpha experimental SAS data
BUNCH model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
...peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 92 nm3

SASDH33 – Rho GTPase-activating protein 22

Rho GTPase-activating protein 22 experimental SAS data
BUNCH model
Sample: Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
...peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 88 nm3

SASDD53 – ...peptide repeat domain of Bacterial cellulose synthesis subunit C

Bacterial cellulose synthesis subunit C experimental SAS data
DAMMIF model
Sample: Bacterial cellulose synthesis subunit C monomer, 71 kDa Enterobacter sp. CJF-002 protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Apr 24
Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C. Sci Rep 7(1):13018 (2017)
Nojima S, Fujishima A, Kato K, Ohuchi K, Shimizu N, Yonezawa K, Tajima K, Yao M
RgGuinier 5.1 nm
Dmax 18.5 nm
VolumePorod 115 nm3

SASDC63 – ...peptide (FPV039:BAK)

Bcl-2-like protein FPV039Uncharacterized protein (BAK1) experimental SAS data
Bcl-2-like protein FPV039 Uncharacterized protein (BAK1) Kratky plot
Sample: Bcl-2-like protein FPV039 monomer, 17 kDa Fowlpox virus protein
Uncharacterized protein (BAK1) monomer, 3 kDa Gallus gallus protein
Buffer: 20 mM trisodium citrate pH, 200 mM NaCl, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Oct 2
Structural basis of apoptosis inhibition by the fowlpox virus protein FPV039. J Biol Chem 292(22):9010-9021 (2017)
Anasir MI, Caria S, Skinner MA, Kvansakul M
RgGuinier 2.0 nm

SASDH83 – Chemically crossed linked complex between Rho GTPase-activating protein 22 (ARHGAP22) and the beta isoform of the 14-3-3 protein beta/alpha

14-3-3 protein beta/alphaRho GTPase-activating protein 22 experimental SAS data
CORAL model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
...peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 195 nm3

SASDJW3 – ...peptide and acyl anchoring cysteine

BON domain protein experimental SAS data
DAMMIF model
Sample: BON domain protein decamer, 229 kDa Acinetobacter baumannii protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 11
BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function. mBio :e0148021 (2021)
Grinter R, Morris FC, Dunstan RA, Leung PM, Kropp A, Belousoff M, Gunasinghe SD, Scott NE, Beckham S, Peleg AY, Greening C, Li J, Heinz E, Lithgow T
RgGuinier 4.7 nm
Dmax 16.4 nm
VolumePorod 546 nm3

SASDJX3 – ...peptide and 27 N-terminal amino acids

BON domain protein experimental SAS data
DAMMIF model
Sample: BON domain protein monomer, 20 kDa Acinetobacter baumannii protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 11
BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function. mBio :e0148021 (2021)
Grinter R, Morris FC, Dunstan RA, Leung PM, Kropp A, Belousoff M, Gunasinghe SD, Scott NE, Beckham S, Peleg AY, Greening C, Li J, Heinz E, Lithgow T
RgGuinier 3.1 nm
Dmax 10.8 nm
VolumePorod 49 nm3

SASDC44 – Envelope of Col H PKD-CBD complexed with mini-collagen

ColH proteinCollagenous Peptide model [(PPG)10] experimental SAS data
DAMMIF model
Sample: ColH protein monomer, 24 kDa Hathewaya histolytica protein
...Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 2.7 nm
Dmax 12.0 nm
VolumePorod 28 nm3

SASDC54 – Envelope of Col H PKD-PKD-CBD complexed with mini-collagen

ColH proteinCollagenous Peptide model [(PPG)10] experimental SAS data
DAMMIF model
Sample: ColH protein monomer, 34 kDa Hathewaya histolytica protein
...Peptide model [(PPG)10] trimer, 10 kDa synthetic construct protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 3.3 nm
Dmax 14.2 nm
VolumePorod 38 nm3

SASDC64 – Envelope of Col G PKD-CBD-CBD complexed with mini-collagen

Collagenous Peptide model [(PPG)10]ColG Collagenase experimental SAS data
DAMMIF model
Sample: ...Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
ColG Collagenase monomer, 37 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 4.1 nm
Dmax 19.3 nm
VolumePorod 70 nm3

SASDJ64 – Calcium bound Calmodulin

Calmodulin-1 experimental SAS data
DENSS model
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 4 mM CaCl₂, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Sep 24
A High‐Affinity Calmodulin‐Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells Advanced Science :2003630 (2021)
Voegele A, Sadi M, O'Brien D, Gehan P, Raoux‐Barbot D, Davi M, Hoos S, Brûlé S, Raynal B, Weber P, Mechaly A, Haouz A, Rodriguez N, Vachette P, Durand D, Brier S, Ladant D, Chenal A
RgGuinier 2.2 nm
Dmax 7.3 nm
VolumePorod 27 nm3

SASDJ74 – ...peptide from B.pertussis CyaA toxin complexed with calmodulin

Calmodulin-1Bifunctional hemolysin/adenylate cyclase experimental SAS data
DENSS model
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Bifunctional hemolysin/adenylate cyclase monomer, 3 kDa Bordetella pertussis protein
Buffer: 20 mM HEPES, 150 mM NaCl, 4 mM CaCl₂, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Sep 24
A High‐Affinity Calmodulin‐Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells Advanced Science :2003630 (2021)
Voegele A, Sadi M, O'Brien D, Gehan P, Raoux‐Barbot D, Davi M, Hoos S, Brûlé S, Raynal B, Weber P, Mechaly A, Haouz A, Rodriguez N, Vachette P, Durand D, Brier S, Ladant D, Chenal A
RgGuinier 2.0 nm
Dmax 7.0 nm
VolumePorod 28 nm3

SASDAN4 – ...peptide complex

CalmodulinC-terminal region of human myelin basic protein experimental SAS data
SASREF model
Sample: Calmodulin monomer, 17 kDa Homo sapiens protein
C-terminal region of human myelin basic protein monomer, 2 kDa Homo sapiens protein
Buffer: 25 mM Tris75 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Nov 28
Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure. BMC Struct Biol 8:10 (2008)
Majava V, Petoukhov MV, Hayashi N, Pirilä P, Svergun DI, Kursula P
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 36 nm3

SASDPN4 – ...Peptide Bound to p120RasGAP's SH2-SH3-SH2 Domains

Ras GTPase-activating protein 1Rho GTPase-activating protein 35 experimental SAS data
DAMMIF model
Sample: Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Rho GTPase-activating protein 35 monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8 350 mM NaCl 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Dec 11
Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP. Structure (2022)
Stiegler AL, Vish KJ, Boggon TJ
RgGuinier 2.4 nm
Dmax 7.9 nm
VolumePorod 41 nm3

SASDNU4 – Di[3-deoxy-D-manno-octulosonyl]-lipid A ammonium salt deposited onto silicon wafer (oriented sample anisotropic scattering, KDO2 control)

Di[3-deoxy-D-manno-octulosonyl]-lipid A (ammonium salt) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Di[3-deoxy-D-manno-octulosonyl]-lipid A (ammonium salt) , unidentified lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 Apr 1
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDAV4 – uPAR wild-type AE105 complex

Urokinase plasminogen activator surface receptorsynthetic peptide AE105 experimental SAS data
Urokinase plasminogen activator surface receptor synthetic peptide AE105 Kratky plot
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
...peptide AE105 monomer, 1 kDa protein
Buffer: 25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Jun 10
A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). J Biol Chem 287(41):34304-15 (2012)
Mertens HD, Kjaergaard M, Mysling S, Gårdsvoll H, Jørgensen TJ, Svergun DI, Ploug M
RgGuinier 2.5 nm
Dmax 8.5 nm
VolumePorod 61 nm3

SASDNV4 – ...peptide WLBU2 (oriented sample anisotropic scattering, KDO2-WLBU2)

Di[3-deoxy-D-manno-octulosonyl]-lipid A (ammonium salt) plus WLBU2 experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Di[3-deoxy-D-manno-octulosonyl]-lipid A (ammonium salt) plus WLBU2 , unidentified lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 Apr 1
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDAW4 – uPAR wild-type AE234 complex

Urokinase plasminogen activator surface receptorsynthetic peptide AE234 experimental SAS data
Urokinase plasminogen activator surface receptor synthetic peptide AE234 Kratky plot
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
...peptide AE234 monomer, 1 kDa protein
Buffer: 25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Jun 10
A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). J Biol Chem 287(41):34304-15 (2012)
Mertens HD, Kjaergaard M, Mysling S, Gårdsvoll H, Jørgensen TJ, Svergun DI, Ploug M
RgGuinier 2.4 nm
Dmax 8.3 nm
VolumePorod 57 nm3

SASDNW4 – Gram-negative bacteria lipid membrane mimic deposited onto silicon wafer (oriented sample anisotropic scattering)

1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol) sodium salt, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phospho]-sn-glycerol (7:2:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol) sodium salt, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phospho]-sn-glycerol (7:2:1) , lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Jun 23
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDNX4 – ...peptide WLBU2 (oriented sample anisotropic scattering)

1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanol, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol) sodium salt, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phospho]-sn-glycerol sodium salt, WLBU2 experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanol, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol) sodium salt, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phospho]-sn-glycerol sodium salt, WLBU2 , synthetic construct lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 Apr 1
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDNY4 – Gram-positive bacteria lipid membrane mimic deposited onto silicon wafer (oriented sample anisotropic scattering)

1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol), 1,2-dioleoyl-3-trimethylammonium-propane, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phos experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol), 1,2-dioleoyl-3-trimethylammonium-propane, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phos , lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 Apr 1
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDNZ4 – ...peptide WLBU2 (oriented sample anisotropic scattering)

1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol), 1,2-dioleoyl-3-trimethylammonium-propane, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phos experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(10-rac-glycerol), 1,2-dioleoyl-3-trimethylammonium-propane, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine, 10,30-bis-[1,2-dioleoyl-sn-glycero-3-phos , synthetic construct lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 Apr 1
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDN25 – Lipopolysaccharide outer membrane of the Gram-negative bacteria Pseudomonas aeruginosa deposited onto silicon wafer (oriented sample anisotropic scattering, LPS control)

Lipopolysaccharide experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Lipopolysaccharide , Pseudomonas aeruginosa lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 Jun 1
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDN35 – ...peptide WLBU2 (LPS-WLBU2, oriented sample anisotropic scattering)

Lipopolysaccharide plus WLBU2 experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Lipopolysaccharide plus WLBU2 dimer, Pseudomonas aeruginosa lipid
Buffer: water, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 Jun 1
...Peptide Mechanism Studied by Scattering-Guided Molecular Dynamics Simulation. J Phys Chem B (2022)
Allsopp R, Pavlova A, Cline T, Salyapongse AM, Gillilan RE, Di YP, Deslouches B, Klauda JB, Gumbart JC, Tristram-Nagle S

SASDG55 – ...peptide, LAP (TGFB-1)

Latency associated peptide experimental SAS data
Latency associated peptide Kratky plot
Sample: ...peptide dimer, 58 kDa Homo sapiens protein
Buffer: phosphate buffered saline 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Apr 20
...peptide between transforming growth factor β-1 bound and unbound states IUCrJ 7(2) (2020)
Stachowski T, Snell M, Snell E
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 129 nm3

SASDG85 – ...peptide complex bound to the CYP7A1 promoter oligonucleotide duplex.

Liver Receptor Homolog-1Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 AlphaCYP7A1 Promoter ForwardCYP7A1 Promoter Reverse experimental SAS data
Liver Receptor Homolog-1 Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha CYP7A1 Promoter Forward CYP7A1 Promoter Reverse Kratky plot
Sample: Liver Receptor Homolog-1 monomer, 64 kDa Homo sapiens protein
Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha monomer, 2 kDa Homo sapiens protein
CYP7A1 Promoter Forward monomer, 4 kDa Homo sapiens DNA
CYP7A1 Promoter Reverse monomer, 4 kDa Homo sapiens DNA
Buffer: 20 mM TRIS, 150 mM NaCl, 2% v/v glycerol, 0.5 mM CHAPS, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 26
Integrated Structural Modeling of Full-Length LRH-1 Reveals Inter-domain Interactions Contribute to Receptor Structure and Function. Structure (2020)
Seacrist CD, Kuenze G, Hoffmann RM, Moeller BE, Burke JE, Meiler J, Blind RD
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 76 nm3

SASDMA5 – ...peptide of the DNA binding domain of CRX)

Cone-rod homeobox protein experimental SAS data
OTHER model
Sample: Cone-rod homeobox protein monomer, 7 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate,100 mM NaCl, and 5 mM imidazole, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Jun 15
Structural and functional analysis of the human Cone-rod homeobox transcription factor. Proteins (2022)
Clanor PB, Buchholz C, Hayes JE, Friedman MA, White AM, Enke RA, Berndsen CE
RgGuinier 1.2 nm
Dmax 4.0 nm
VolumePorod 10 nm3

SASDGB5 – ...peptide

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.0 nm
Dmax 13.1 nm
VolumePorod 32 nm3

SASDGC5 – ...peptide (diluted)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 5 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.6 nm
Dmax 12.4 nm
VolumePorod 32 nm3

SASDGD5 – ...peptide (Paused SEC)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.3 nm
Dmax 6.8 nm
VolumePorod 28 nm3

SASDGE5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 9.2 nm
VolumePorod 32 nm3

SASDGF5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (diluted)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.5 nm
Dmax 9.5 nm
VolumePorod 32 nm3

SASDGG5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (Paused SEC)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 6.4 nm
VolumePorod 31 nm3

SASDGH5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.7 nm
Dmax 6.3 nm
VolumePorod 29 nm3

SASDGJ5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (diluted)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 16 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.1 nm
Dmax 7.0 nm
VolumePorod 41 nm3

SASDGK5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (Paused SEC)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 7.2 nm
VolumePorod 30 nm3

SASDML5 – ...peptides loaded with M1 protein

Proteoliposomes composed of lipids from A/Puerto Rico/8/34 (H1N1) virus envelope together with the HA LI45 peptides loaded with M1 protein (lipid:M1 molar ration 4:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: ...peptides loaded with M1 protein (lipid:M1 molar ration 4:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 26
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
Kordyukova L, Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDVL5 – Small EDRK-rich factor 1 (SERF1a)

Isoform Short of Small EDRK-rich factor 1 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Mar 11
...peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.4 nm
Dmax 8.0 nm
VolumePorod 9 nm3

SASDTM5 – ...peptide

NHLP leader peptide family natural product (I56V) experimental SAS data
NHLP leader peptide family natural product (I56V) Kratky plot
Sample: ...peptide family natural product (I56V) monomer, 9 kDa Methylovulum psychrotolerans protein
Buffer: 20 mM sodium phosphate (pH 7.5), 100 mM NaCl and 48 µM FAD, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, Pennsylvania State University on 2023 Jul 28
...peptides guide post-translational modification by a flavin-dependent RiPP brominase. Nat Commun 15(1):1265 (2024)
Nguyen NA, Vidya FNU, Yennawar NH, Wu H, McShan AC, Agarwal V
RgGuinier 1.9 nm
Dmax 5.5 nm
VolumePorod 39 nm3

SASDVM5 – ...peptide

HTT3 experimental SAS data
ROSETTA model
Sample: HTT3 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 May 20
...peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.0 nm

SASDVN5 – ...peptide

NT17 experimental SAS data
ROSETTA model
Sample: NT17 monomer, 2 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Oct 21
...peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 1.2 nm
Dmax 4.0 nm
VolumePorod 5 nm3

SASDVP5 – ...peptide

HTT0 experimental SAS data
ROSETTA model
Sample: HTT0 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2023 Nov 10
...peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 1.5 nm
Dmax 6.0 nm
VolumePorod 4 nm3

SASDHQ5 – ...peptide self-assembly

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data
OTHER model
Sample: ...peptide , 1 kDa synthetic construct protein
Buffer: pure (MQ, 18 MΩ) Water, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Nov 1
Amyloid Evolution: Antiparallel Replaced by Parallel. Biophys J (2020)
Zanjani AAH, Reynolds NP, Zhang A, Schilling T, Mezzenga R, Berryman JT

SASDLQ5 – Tricorn protease oligomers

Tricorn protease experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tricorn protease hexamer, 730 kDa Thermoplasma acidophilum (strain … protein
Buffer: 20mM Tris-HCl, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2003 Jan 14
...peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum. J Biol Chem 280(39):33387-96 (2005)
Goettig P, Brandstetter H, Groll M, Göhring W, Konarev PV, Svergun DI, Huber R, Kim JS
RgGuinier 5.9 nm

SASDVQ5 – ...peptide

HTT1 experimental SAS data
HTT1 Kratky plot
Sample: HTT1 dimer, 8 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Feb 3
...peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 18 nm3

SASDVR5 – ...peptide

Isoform Short of Small EDRK-rich factor 1NT17 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
NT17 dimer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Oct 21
...peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm

SASDVS5 – ...peptide

Isoform Short of Small EDRK-rich factor 1HTT3 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
HTT3 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 May 20
...peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm
Dmax 7.2 nm
VolumePorod 9 nm3

SASDA66 – BAZ2B-18mer complex in Tris

Bromodomain adjacent to zinc finger domain protein 2B, C-terminalH3Kac9Kac14 experimental SAS data
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal H3Kac9Kac14 Kratky plot
Sample: Bromodomain adjacent to zinc finger domain protein 2B, C-terminal monomer, 28 kDa Homo sapiens protein
H3Kac9Kac14 monomer, 5 kDa Homo sapiens protein
Buffer: 20 mM Tris 500 mM NaCl 2 mM DTT 10 microM ZnCl2, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 24
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. Structure 23(1):80-92 (2015)
Tallant C, Valentini E, Fedorov O, Overvoorde L, Ferguson FM, Filippakopoulos P, Svergun DI, Knapp S, Ciulli A
RgGuinier 4.2 nm
Dmax 16.0 nm
VolumePorod 52 nm3

SASDJA6 – Complement C5

Complement C5 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Complement C5 monomer, 186 kDa Homo sapiens protein
Buffer: 20mM Tris pH, 75mM NaCl, and 3% glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 12
...peptides. Elife 10 (2021)
Macpherson A, Laabei M, Ahdash Z, Graewert MA, Birtley JR, Schulze ME, Crennell S, Robinson SA, Holmes B, Oleinikovas V, Nilsson PH, Snowden J, Ellis V, Mollnes TE, Deane CM, Svergun D, Lawson AD, van...
RgGuinier 4.8 nm
Dmax 17.6 nm
VolumePorod 392 nm3

SASDJS6 – ...peptide [(POG)10]3

Collagenous Peptide model [(PPG)10]Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) experimental SAS data
DAMFILT model
Sample: ...Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) monomer, 23 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Dec 12
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in... University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 3.5 nm
Dmax 14.5 nm
VolumePorod 41 nm3

SASDJT6 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser, Phe712Ser, Tyr780Ser, His782Ser, Tyr796Ser and Tyr801) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser, Phe712Ser, Tyr780Ser, His782Ser, Tyr796Ser and Tyr801) monomer, 33 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in... University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 4.0 nm
Dmax 22.0 nm
VolumePorod 61 nm3

SASDJV6 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser and Phe712Ser) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser and Phe712Ser) monomer, 33 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Dec 12
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in... University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 4.4 nm
Dmax 21.0 nm
VolumePorod 79 nm3

SASDJX6 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) monomer, 34 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in... University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 4.0 nm
Dmax 22.0 nm
VolumePorod 63 nm3

SASDKX6 – ...peptide from Chrysomya megacephala

PSK, an antimicrobial peptide from Chrysomya megacephala experimental SAS data
DAMMIF model
Sample: ...peptide from Chrysomya megacephala monomer, 10 kDa Chrysomya megacephala protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Dec 7
...peptide from Chrysomya megacephala. Acta Crystallogr D Struct Biol 77(Pt 7):894-903 (2021)
Xiao C, Xiao Z, Hu C, Lu J, Cui L, Zhang Y, Dai Y, Zhang Q, Wang S, Liu W
RgGuinier 1.6 nm
Dmax 5.0 nm
VolumePorod 18 nm3

SASDJ27 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser) monomer, 23 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in... University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 3.2 nm
Dmax 18.0 nm
VolumePorod 34 nm3

SASDJ37 – ...peptide

Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD))Collagen like-peptide [GPRG(POG)13] experimental SAS data
DAMFILT model
Sample: Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) monomer, 23 kDa Hathewaya histolytica protein
...peptide [GPRG(POG)13] trimer, 11 kDa protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in... University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 3.3 nm
Dmax 18.0 nm
VolumePorod 35 nm3

SASDQ87 – Solution structure of colibactin ClbK

Colibactin hybrid non-ribosomal peptide synthetase/type I polyketide synthase ClbK experimental SAS data
Colibactin hybrid non-ribosomal peptide synthetase/type I polyketide synthase ClbK Kratky plot
Sample: ...peptide synthetase/type I polyketide synthase ClbK dimer, 476 kDa Escherichia coli protein
Buffer: 50 mM Hepes pH 7.5, 200 mM NaCl, 5 mM DTT, 5 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2020 Sep 14
Architecture of a PKS-NRPS hybrid megaenzyme involved in the biosynthesis of the genotoxin colibactin Structure (2023)
Bonhomme S, Contreras-Martel C, Dessen A, Macheboeuf P
RgGuinier 8.0 nm
Dmax 30.0 nm
VolumePorod 1340 nm3

SASDTS7 – Bovine Lactoferrin

Lactoferrin experimental SAS data
Lactoferrin Kratky plot
Sample: Lactoferrin monomer, 75 kDa Bos taurus protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
...peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 117 nm3

SASDTT7 – Lactoferrin binding protein B

Transferrin-binding protein B experimental SAS data
Transferrin-binding protein B Kratky plot
Sample: Transferrin-binding protein B monomer, 97 kDa Moraxella bovis protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
...peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 3.7 nm
Dmax 12.4 nm
VolumePorod 130 nm3

SASDTU7 – Lactoferrin binding protein B (C-terminal alpha helical domain)

Transferrin-binding protein B experimental SAS data
Transferrin-binding protein B Kratky plot
Sample: Transferrin-binding protein B monomer, 32 kDa Moraxella bovis protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
...peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 3.2 nm
Dmax 11.9 nm
VolumePorod 49 nm3

SASDUU7 – ...peptide

Tyrosine-protein kinase SYKHigh affinity immunoglobulin epsilon receptor subunit gamma experimental SAS data
Tyrosine-protein kinase SYK High affinity immunoglobulin epsilon receptor subunit gamma Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
High affinity immunoglobulin epsilon receptor subunit gamma monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 54 nm3

SASDTV7 – Lactoferrin binding protein B (C-terminal alpha helical domain) bound to bovine lactoferrin

LactoferrinTransferrin-binding protein B experimental SAS data
Lactoferrin Transferrin-binding protein B Kratky plot
Sample: Lactoferrin monomer, 75 kDa Bos taurus protein
Transferrin-binding protein B monomer, 32 kDa Moraxella bovis protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
...peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 5.6 nm
Dmax 20.3 nm
VolumePorod 318 nm3

SASDUV7 – ...peptide

Tyrosine-protein kinase SYKT-cell surface glycoprotein CD3 gamma chain experimental SAS data
Tyrosine-protein kinase SYK T-cell surface glycoprotein CD3 gamma chain Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
T-cell surface glycoprotein CD3 gamma chain monomer, 3 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 56 nm3

SASDUW7 – ...peptide

Tyrosine-protein kinase SYKTYRO protein tyrosine kinase-binding protein experimental SAS data
Tyrosine-protein kinase SYK TYRO protein tyrosine kinase-binding protein Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
TYRO protein tyrosine kinase-binding protein monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 53 nm3

SASDAE8 – ...peptide

Human Filamin A Ig-like domains 20-21/migfilin peptide complex experimental SAS data
Human Filamin A Ig-like domains 20-21/migfilin peptide complex Kratky plot
Sample: ...peptide complex monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 31 nm3

SASDAF8 – Human Filamin A Ig-like domains 20-21 truncation (2151-2329)

Human Filamin A Ig-like domains 20-21 experimental SAS data
Human Filamin A Ig-like domains 20-21 Kratky plot
Sample: Human Filamin A Ig-like domains 20-21 monomer, 19 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.5 nm
VolumePorod 29 nm3

SASDHF8 – ...peptide) at 4.89 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K

Histatin-3, His3-(20-43)-peptide experimental SAS data
Histatin 5 (Histatin 3; His3-(20-43)-peptide) at 4.89 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K Rg histogram
Sample: ...peptide monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl,, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 13
Comment on the Optimal Parameters to Derive Intrinsically Disordered Protein Conformational Ensembles from Small-Angle X-ray Scattering Data Using the Ensemble Optimization Method Journal of Chemical Theory and Computation (2021)
Sagar A, Jeffries C, Petoukhov M, Svergun D, Bernadó P
RgGuinier 1.4 nm
Dmax 6.0 nm
VolumePorod 3 nm3

SASDAG8 – ...peptide

Human Filamin A Ig-like domains 20-21*/migfilin peptide complex experimental SAS data
Human Filamin A Ig-like domains 20-21*/migfilin peptide complex Kratky plot
Sample: ...peptide complex monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 33 nm3

SASDHG8 – ...peptide) at 2.51 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K

Histatin-3, His3-(20-43)-peptide experimental SAS data
Histatin-3, His3-(20-43)-peptide Kratky plot
Sample: ...peptide monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 13
Comment on the Optimal Parameters to Derive Intrinsically Disordered Protein Conformational Ensembles from Small-Angle X-ray Scattering Data Using the Ensemble Optimization Method Journal of Chemical Theory and Computation (2021)
Sagar A, Jeffries C, Petoukhov M, Svergun D, Bernadó P
RgGuinier 1.5 nm
Dmax 6.4 nm
VolumePorod 3 nm3

SASDAH8 – Human Filamin A Ig-like domains 20-21* truncation (2141-2329)

Human Filamin A Ig-like domains 20-21* experimental SAS data
DAMMIF model
Sample: Human Filamin A Ig-like domains 20-21* monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 1.9 nm
Dmax 6.8 nm
VolumePorod 32 nm3

SASDHH8 – ...peptide) at 1.26 mg/ml in 20 mM Tris 150 mM NaCl pH 7.0, 298 K

Histatin-3, His3-(20-43)-peptide experimental SAS data
Histatin-3, His3-(20-43)-peptide Kratky plot
Sample: ...peptide monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 13
Comment on the Optimal Parameters to Derive Intrinsically Disordered Protein Conformational Ensembles from Small-Angle X-ray Scattering Data Using the Ensemble Optimization Method Journal of Chemical Theory and Computation (2021)
Sagar A, Jeffries C, Petoukhov M, Svergun D, Bernadó P
RgGuinier 1.5 nm
Dmax 6.0 nm
VolumePorod 3 nm3

SASDHK8 – ...peptide self-assembly (2019-dataset)

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data
Ile-Leu-Gln-Ile-Asn-Ser peptide Kratky plot
Sample: ...peptide , 1 kDa synthetic construct protein
Buffer: pure (MQ, 18 MΩ) Water, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Nov 1
Amyloid Evolution: Antiparallel Replaced by Parallel. Biophys J (2020)
Zanjani AAH, Reynolds NP, Zhang A, Schilling T, Mezzenga R, Berryman JT

SASDDT8 – ...peptide 5 (DILP5)

Insulin-like peptide 5Neural/ectodermal development factor IMP-L2 experimental SAS data
Insulin-like peptide 5 Neural/ectodermal development factor IMP-L2 Kratky plot
Sample: ...peptide 5 monomer, 5 kDa Drosophila melanogaster protein
Neural/ectodermal development factor IMP-L2 monomer, 30 kDa Drosophila melanogaster protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 20
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Nat Commun 9(1):3860 (2018)
Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 55 nm3

SASDKT8 – ...peptide 3mg/ml

von Willebrand factor experimental SAS data
von Willebrand factor Kratky plot
Sample: von Willebrand factor monomer, 11 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 24
An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution. J Mol Biol 433(13):166954 (2021)
Del Amo-Maestro L, Sagar A, Pompach P, Goulas T, Scavenius C, Ferrero DS, Castrillo-Briceño M, Taulés M, Enghild JJ, Bernadó P, Gomis-Rüth FX
RgGuinier 3.1 nm
Dmax 14.0 nm
VolumePorod 28 nm3

SASDKU8 – ...peptide 6mg/ml

von Willebrand factor experimental SAS data
von Willebrand Factor peptide 6mg/ml Rg histogram
Sample: von Willebrand factor monomer, 11 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 24
An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution. J Mol Biol 433(13):166954 (2021)
Del Amo-Maestro L, Sagar A, Pompach P, Goulas T, Scavenius C, Ferrero DS, Castrillo-Briceño M, Taulés M, Enghild JJ, Bernadó P, Gomis-Rüth FX
RgGuinier 3.0 nm
Dmax 14.9 nm
VolumePorod 27 nm3

SASDKV8 – ...peptide

von Willebrand factorA disintegrin and metalloproteinase with thrombospondin motifs 13 experimental SAS data
ADAMTS-13 bound to von Willebrand Factor peptide Rg histogram
Sample: von Willebrand factor monomer, 11 kDa Homo sapiens protein
A disintegrin and metalloproteinase with thrombospondin motifs 13 monomer, 70 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 24
An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution. J Mol Biol 433(13):166954 (2021)
Del Amo-Maestro L, Sagar A, Pompach P, Goulas T, Scavenius C, Ferrero DS, Castrillo-Briceño M, Taulés M, Enghild JJ, Bernadó P, Gomis-Rüth FX
RgGuinier 4.4 nm
Dmax 16.3 nm
VolumePorod 170 nm3

SASDCW8 – ...peptide @ 4mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 46 nm3

SASDCX8 – ...peptide @ 6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 47 nm3

SASDCY8 – ...peptide @ 8mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 46 nm3

SASDCZ8 – ...peptide @ 12.2 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.8 nm

SASDC29 – ...peptide @ 10.6 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
HADDOCK model
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm
Dmax 11.0 nm
VolumePorod 108 nm3

SASDC39 – ...peptide @ 9.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
HADDOCK model
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.0 nm
Dmax 11.4 nm
VolumePorod 107 nm3

SASDC49 – ...peptide @ 6.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.1 nm
Dmax 11.6 nm
VolumePorod 105 nm3

SASDC59 – ...peptide @ 7.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm
Dmax 11.1 nm
VolumePorod 106 nm3

SASDC69 – ...peptide @ 4.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm

SASDC79 – ...peptide @ 3.0mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.8 nm

SASDC89 – ...peptide @ 1.5 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.7 nm

SASDHU5 – Heat shock protein 70 (PfHSP70-1)

Heat shock protein 70Peptide experimental SAS data
DAMFILT model
Sample: Heat shock protein 70 monomer, 74 kDa Plasmodium falciparum protein
Peptide monomer, 1 kDa synthetic construct protein
Buffer: 50mM Tris, 5mM MgCl2, 500mM KCl, 5mM Bme, 5% glycerol, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 Oct 24
Structural-functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding. Biochem J 477(18):3625-3643 (2020)
Anas M, Shukla A, Tripathi A, Kumari V, Prakash C, Nag P, Kumar LS, Sharma SK, Ramachandran R, Kumar N
RgGuinier 5.3 nm
Dmax 16.6 nm
VolumePorod 450 nm3

SASDRS7 – ...peptide epimerase in the presence of SAM (S-adenosyl-L-methionine)

Putative peptide biosynthesis protein YydG experimental SAS data
DADIMODO model
Sample: ...peptide biosynthesis protein YydG dimer, 80 kDa Bacillus subtilis (strain … protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Nov 29
Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme. Nat Chem Biol (2023)
Kubiak X, Polsinelli I, Chavas LMG, Fyfe CD, Guillot A, Fradale L, Brewee C, Grimaldi S, Gerbaud G, Thureau A, Legrand P, Berteau O, Benjdia A
RgGuinier 2.9 nm
Dmax 11.8 nm
VolumePorod 115 nm3

SASDRK6 – ...peptide

Ephrin type-B receptor 4Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) experimental SAS data
Ephrin type-B receptor 4 Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) Kratky plot
Sample: Ephrin type-B receptor 4 monomer, 2 kDa Homo sapiens protein
Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 350 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Dec 12
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 2.7 nm
Dmax 10.5 nm
VolumePorod 44 nm3

SASDRR7 – ...peptide epimerase in the presence of SAM (S-adenosyl-L-methionine) and a peptide subtrate

Putative peptide biosynthesis protein YydG experimental SAS data
DADIMODO model
Sample: ...peptide biosynthesis protein YydG dimer, 80 kDa Bacillus subtilis (strain … protein
Buffer: 25 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Nov 30
Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme. Nat Chem Biol (2023)
Kubiak X, Polsinelli I, Chavas LMG, Fyfe CD, Guillot A, Fradale L, Brewee C, Grimaldi S, Gerbaud G, Thureau A, Legrand P, Berteau O, Benjdia A
RgGuinier 2.9 nm
Dmax 12.0 nm
VolumePorod 113 nm3

SASDJG6 – ...peptide

The separated apo-linker region peptide from the plant Cicer arietinum experimental SAS data
The separated apo-linker region peptide Rg histogram
Sample: ...peptide from the plant Cicer arietinum monomer, 4 kDa Cicer arietinum protein
Buffer: 10 mM Tris, 50 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 8
Structural Characterization of Plant Metallothionein
Dima Molodenskiy
RgGuinier 1.4 nm
Dmax 6.5 nm
VolumePorod 1 nm3

SASDRL6 – ...peptide

Rho GTPase-activating protein 35Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) experimental SAS data
Rho GTPase-activating protein 35 Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) Kratky plot
Sample: Rho GTPase-activating protein 35 monomer, 3 kDa Homo sapiens protein
Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 350 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Dec 12
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 2.4 nm
Dmax 7.7 nm
VolumePorod 44 nm3

SASDRF6 – ...peptide

Ephrin type-B receptor 4Ras GTPase-activating protein 1 experimental SAS data
Ephrin type-B receptor 4 Ras GTPase-activating protein 1 Kratky plot
Sample: Ephrin type-B receptor 4 monomer, 2 kDa Homo sapiens protein
Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 3.9 nm
Dmax 13.7 nm
VolumePorod 176 nm3