Small Angle Scattering Biological Data Bank SASBDB


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45 hits found for Stokes

SASDM42 – Cobalt/magnesium transport protein CorA in matched-out deuterated dodecylmaltoside (dDDM) micelles without Mg2+

Cobalt/magnesium transport protein CorA experimental SAS data

Cobalt/magnesium transport protein CorA Kratky plot

Sample:	Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer:	20 mM Tris-DCl, 150 mM NaCl, 1 mM EDTA-NaOD, in 100% D2O, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23

Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation. Elife 11 (2022)
Johansen NT, Bonaccorsi M, Bengtsen T, Larsen AH, Tidemand FG, Pedersen MC, Huda P, Berndtsson J, Darwish T, Yepuri NR, Martel A, Pomorski TG, Bertarello A, Sansom M, Rapp M, Crehuet R, Schubeis T, Li...

R_g^Guinier	4.2	nm
D_max	13.9	nm

SASDM52 – Cobalt/magnesium transport protein CorA in matched-out deuterated dodecylmaltoside (dDDM) micelles with bound Mg2+

Sample:	Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer:	20 mM Tris-DCl, 150 mM NaCl, 40 mM MgCl2, in 100% D2O, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23

R_g^Guinier	4.3	nm
D_max	13.9	nm

SASDM62 – Cobalt/magnesium transport protein CorA in matched-out deuterated nanodiscs without Mg2+

Sample:	Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer:	20 mM Tris-DCl, 150 mM NaCl, 1 mM EDTA-NaOD, in 100% D2O, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23

R_g^Guinier	4.8	nm
D_max	14.2	nm

SASDM72 – Cobalt/magnesium transport protein CorA in match-out deuterated nanodiscs with bound Mg2+

Sample:	Cobalt/magnesium transport protein CorA pentamer, 208 kDa Thermotoga maritima (strain … protein
Buffer:	20 mM Tris-DCl, 150 mM NaCl, 40 mM MgCl2, in 100% D2O, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 23

R_g^Guinier	4.9	nm
D_max	14.3	nm

SASDNK2 – Circadian clock hKaiA-75dKaiB-75dKaiC ternary protein complex measured by SEC-SANS in 100% D2O

75% deuterated Circadian clock protein KaiBCircadian clock protein KaiA75% deuterated Circadian clock protein kinase KaiC (S431D mutant) experimental SAS data

Sample:	75% deuterated Circadian clock protein KaiB hexamer, 71 kDa Synechococcus elongatus (strain … protein Circadian clock protein KaiA dodecamer, 393 kDa Synechococcus elongatus (strain … protein 75% deuterated Circadian clock protein kinase KaiC (S431D mutant) hexamer, 357 kDa Synechococcus elongatus (strain … protein
Buffer:	50 mM sodium phosphate buffer, 150 mm NaCl, 5 mM MgCl2, 0.5 mM EDTA, 1 mM ATP, 1 mM DTT, 50 mM arginine, 50 mM glutamine, in 100% D2O, pH: 7.8
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Sep 19

Overall structure of fully assembled cyanobacterial KaiABC circadian clock complex by an integrated experimental-computational approach. Commun Biol 5(1):184 (2022)
Yunoki Y, Matsumoto A, Morishima K, Martel A, Porcar L, Sato N, Yogo R, Tominaga T, Inoue R, Yagi-Utsumi M, Okuda A, Shimizu M, Urade R, Terauchi K, Kono H, Yagi H, Kato K, Sugiyama M

R_g^Guinier	7.8	nm
D_max	25.6	nm
Volume^Porod	1620	nm³

SASDGW2 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H L7Ae, 1H st-sR26 RNA, 1H substrate D' and 2H Nop5 (SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Sep 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.1	nm
D_max	14.0	nm
Volume^Porod	210	nm³

SASDGX2 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H Nop5, 1H st-sR26 RNA, 1H substrate D' and 2H L7Ae (SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Nov 23

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.0	nm
D_max	13.3	nm
Volume^Porod	42	nm³

SASDGY2 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H Nop5, 1H L7Ae, 1H substrate D' and 2H st-sR26 RNA (SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jul 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	2.8	nm
D_max	9.9	nm
Volume^Porod	52	nm³

SASDG23 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H L7Ae, 1H substrate D', 2H(70%) Nop5 and 2H st-sR26 RNA (SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Apr 8

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.0	nm
D_max	13.8	nm
Volume^Porod	214	nm³

SASDG33 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H L7Ae, 1H substrate D, 2H(70%) Nop5 and 2H st-sR26 RNA (SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Apr 8

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.0	nm
D_max	13.9	nm
Volume^Porod	231	nm³

SASDL33 – Gloeobacter violaceus Ligand-Gated Ion Channel (GLIC) at pH 7.5 measured with paused-flow SEC-SANS

Proton-gated ion channel experimental SAS data

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Aug 22

Probing solution structure of the pentameric ligand-gated ion channel GLIC by small-angle neutron scattering Proceedings of the National Academy of Sciences 118(37):e2108006118 (2021)
Lycksell M, Rovšnik U, Bergh C, Johansen N, Martel A, Porcar L, Arleth L, Howard R, Lindahl E

R_g^Guinier	3.8	nm
D_max	13.5	nm
Volume^Porod	274	nm³

SASDL43 – Gloeobacter violaceus Ligand-Gated Ion Channel (GLIC) at pH 3.0 measured with paused-flow SEC-SANS

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM citrate, 150 mM NaCl, 0.5 mM match-out deuterated DDM, pH: 3
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Aug 22

R_g^Guinier	3.8	nm
D_max	12.7	nm
Volume^Porod	279	nm³

SASDG53 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Nop5, 1H L7Ae, 1H st-sR26 RNA, 1H substrate D and 2H Nop5 (SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Sep 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.1	nm
D_max	14.0	nm
Volume^Porod	222	nm³

SASDL53 – Gloeobacter violaceus Ligand-Gated Ion Channel (GLIC) at pH 7.5 measured with continuous-flow SEC-SANS

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jun 20

R_g^Guinier	3.8	nm
D_max	12.0	nm
Volume^Porod	235	nm³

SASDG63 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H Nop5, 1H st-sR26 RNA, 1H substrate D and 2H L7Ae (SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Nov 23

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	3.9	nm
D_max	12.5	nm
Volume^Porod	49	nm³

SASDJ63 – Streptococcus pneumoniae NADPH oxidase - Tag-free SpNOX

FAD-binding FR-type domain-containing protein experimental SAS data

Sample:	FAD-binding FR-type domain-containing protein monomer, 47 kDa Streptococcus pneumoniae protein
Buffer:	50 mM Tris-HCl pH 7, 300 mM NaCl, 5 mM LMNG, 10 µM FAD, 21.4% D₂O, pH: 7
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 26

Interdomain Flexibility within NADPH Oxidase Suggested by SANS Using LMNG Stealth Carrier. Biophys J 119(3):605-618 (2020)
Vermot A, Petit-Härtlein I, Breyton C, Le Roy A, Thépaut M, Vivès C, Moulin M, Härtlein M, Grudinin S, Smith SME, Ebel C, Martel A, Fieschi F

R_g^Guinier	3.0	nm
D_max	10.0	nm
Volume^Porod	89	nm³

SASDL63 – Gloeobacter violaceus Ligand-Gated Ion Channel (GLIC) at pH 7.5 measured with cuvette-mode SANS

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jun 21

R_g^Guinier	4.0	nm
D_max	17.7	nm
Volume^Porod	225	nm³

SASDG73 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H Nop5, 1H L7Ae, 1H substrate D and 2H st-sR26 RNA (SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jul 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	2.7	nm
D_max	9.5	nm
Volume^Porod	25	nm³

SASDFP3 – Complex with 1H histone chaperone Asf1, acetyltransferase Rtt109 and histones H3 and H4, 70%-2H histone chaperone Vps75 (1H Asf1-H3:H4-Rtt109, 2H(70%) Vps75) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data

Sample:	Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer:	50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 May 29

Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T

R_g^Guinier	2.8	nm
D_max	9.5	nm

SASDDQ4 – LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) of Insulin gene enhancer protein ISL-2

LIM/homeobox protein Lhx4Insulin gene enhancer protein ISL-2 experimental SAS data

Sample:	LIM/homeobox protein Lhx4 monomer, 15 kDa Mus musculus protein Insulin gene enhancer protein ISL-2 monomer, 4 kDa Mus musculus protein
Buffer:	20 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Nov 19

Mutation in a flexible linker modulates binding affinity for modular complexes. Proteins (2019)
Stokes PH, Robertson NO, Silva AP, Estephan T, Trewhella J, Guss JM, Matthews JM

R_g^Guinier	2.2	nm
D_max	8.0	nm
Volume^Porod	20	nm³

SASDDR4 – LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) R282G mutant of Insulin gene enhancer protein ISL-2

LIM/homeobox protein Lhx4Insulin gene enhancer protein ISL-2 (R282G) experimental SAS data

Sample:	LIM/homeobox protein Lhx4 monomer, 15 kDa Mus musculus protein Insulin gene enhancer protein ISL-2 (R282G) monomer, 4 kDa Mus musculus protein
Buffer:	20 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Nov 19

Mutation in a flexible linker modulates binding affinity for modular complexes. Proteins (2019)
Stokes PH, Robertson NO, Silva AP, Estephan T, Trewhella J, Guss JM, Matthews JM

R_g^Guinier	2.3	nm
D_max	8.5	nm
Volume^Porod	21	nm³

SASDNG5 – Desulfofustis sp. PB-SRB1 ligand-gated ion channel with calcium measured by paused-flow SEC-SANS

Neurotransmitter-gated ion-channel ligand-binding domain-containing protein experimental SAS data

Sample:	Neurotransmitter-gated ion-channel ligand-binding domain-containing protein pentamer, 342 kDa Desulfofustis sp. PB-SRB1 protein
Buffer:	20 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.5 mM deuterated n-Dodecyl-B-D-Maltoside, in D2O, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Aug 23

Biophysical characterization of calcium-binding and modulatory-domain dynamics in a pentameric ligand-gated ion channel. Proc Natl Acad Sci U S A 119(50):e2210669119 (2022)
Lycksell M, Rovšnik U, Hanke A, Martel A, Howard RJ, Lindahl E

R_g^Guinier	5.2	nm
D_max	16.8	nm
Volume^Porod	530	nm³

SASDNH5 – Desulfofustis sp. PB-SRB1 ligand-gated ion channel without calcium measured by paused-flow SEC-SANS

Neurotransmitter-gated ion-channel ligand-binding domain-containing protein Kratky plot

Sample:	Neurotransmitter-gated ion-channel ligand-binding domain-containing protein pentamer, 342 kDa Desulfofustis sp. PB-SRB1 protein
Buffer:	20 mM Tris, 150 mM NaCl, 10 mM EDTA, 0.5 mM deuterated n-Dodecyl-B-D-Maltoside, in D2O, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Aug 23

R_g^Guinier	5.2	nm
D_max	16.7	nm
Volume^Porod	540	nm³

SASDL97 – Ru-MtrCAB complex formed by reconstitution of Ru-MtrC and MtrAB

Extracelllular iron oxide respiratory system periplasmic decaheme cytochrome c component MtrAExtracellular iron oxide respiratory system surface decaheme cytochrome c component MtrCExtracellular iron oxide respiratory system outer membrane component MtrB experimental SAS data

Sample:	Extracelllular iron oxide respiratory system periplasmic decaheme cytochrome c component MtrA monomer, 39 kDa Shewanella oneidensis (strain … protein Extracellular iron oxide respiratory system surface decaheme cytochrome c component MtrC monomer, 77 kDa Shewanella oneidensis (strain … protein Extracellular iron oxide respiratory system outer membrane component MtrB monomer, 75 kDa Shewanella oneidensis (strain … protein
Buffer:	20 mM HEPES, 100 mM NaCl, 2.8 mM Fos-choline 12, 13% D2O, pH: 7.8
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Jan 13

Bespoke Biomolecular Wires for Transmembrane Electron Transfer: Spontaneous Assembly of a Functionalized Multiheme Electron Conduit Frontiers in Microbiology 12 (2021)
Piper S, Edwards M, van Wonderen J, Casadevall C, Martel A, Jeuken L, Reisner E, Clarke T, Butt J

R_g^Guinier	4.7	nm
D_max	16.6	nm
Volume^Porod	154	nm³

SASDLA7 – Outer membrane protein complex MtrCAB

Sample:	Extracelllular iron oxide respiratory system periplasmic decaheme cytochrome c component MtrA monomer, 39 kDa Shewanella oneidensis (strain … protein Extracellular iron oxide respiratory system outer membrane component MtrB monomer, 75 kDa Shewanella oneidensis (strain … protein Extracellular iron oxide respiratory system surface decaheme cytochrome c component MtrC monomer, 75 kDa Shewanella oneidensis (strain … protein
Buffer:	20 mM HEPES, 100 mM NaCl, 2.8 mM Fos-choline 12, 13% D2O, pH: 7.8
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Sep 12

R_g^Guinier	5.2	nm
D_max	17.1	nm
Volume^Porod	234	nm³

SASDFK7 – Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O

Sample:	Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer:	50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14

Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T

R_g^Guinier	1.9	nm
D_max	5.5	nm

SASDFL7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data

Sample:	Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer:	50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14

R_g^Guinier	3.4	nm
D_max	10.5	nm

SASDFM7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, acetylatransferase Rtt109, 2H histone chaperone Vps75 (1-225aa) in 42% v/v D2O

Sample:	Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer:	50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14

R_g^Guinier	2.7	nm
D_max	9.0	nm

SASDFN7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4, histone chaperones Asf1 and Vps75 (1-225aa) (acquired in 100% v/v D2O)

Sample:	Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer:	50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 May 30

R_g^Guinier	3.5	nm
D_max	11.0	nm

SASDFP7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O

Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-lengthVacuolar protein sorting-associated protein 75 full-length experimental SAS data

Sample:	Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein
Buffer:	50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9

R_g^Guinier	3.5	nm
D_max	11.5	nm

SASDFQ7 – Complex with 1H histone chaperone Vps75, histones H3 and H4, 2H histone chaperone Asf1, histone acetyltransferase Rtt109, acquired in 42% v/v D2O

Sample:	Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein
Buffer:	50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9

R_g^Guinier	3.1	nm
D_max	9.5	nm

SASDMH9 – Pseudomonas aeruginosa Multidrug resistance operon repressor (MexR) in complex with 34bp dsDNA binding sequence (SANS data at 0% D2O)

Multidrug resistance operon repressor34 base pair double-stranded DNA experimental SAS data

Sample:	Multidrug resistance operon repressor dimer, 32 kDa Pseudomonas aeruginosa protein 34 base pair double-stranded DNA monomer, 21 kDa synthetic construct DNA
Buffer:	20mM NaPO4, 150 mM NaCl, 10 mM DTT, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 May 30

Small-angle X-ray and neutron scattering of MexR and its complex with DNA supports a conformational selection binding model Biophysical Journal (2022)
Caporaletti F, Pietras Z, Morad V, Mårtensson L, Gabel F, Wallner B, Martel A, Sunnerhagen M

R_g^Guinier	2.9	nm
D_max	7.8	nm
Volume^Porod	79	nm³

SASDDJ9 – Conformation of the R1-3 human dystrophin fragment (SANS)

R1-3 human dystrophin fragment experimental SAS data

Sample:	R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7

Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF

R_g^Guinier	4.2	nm
D_max	17.7	nm
Volume^Porod	46	nm³

SASDDK9 – Conformation of R1-3 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

Sample:	R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7

R_g^Guinier	4.1	nm
D_max	17.8	nm
Volume^Porod	50	nm³

SASDDL9 – Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Sample:	R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7

R_g^Guinier	6.2	nm
D_max	24.8	nm
Volume^Porod	100	nm³

SASDPA4 – SAXS data for the trimeric C-phycocyanin

C-phycocyanin alpha subunitC-phycocyanin beta subunit experimental SAS data

Sample:	C-phycocyanin alpha subunit trimer, 53 kDa Arthrospira platensis protein C-phycocyanin beta subunit trimer, 54 kDa Arthrospira platensis protein
Buffer:	150 mM NaCl, 20 mM Tris, pH: 7.6
Experiment:	SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2022 Apr 14

...Stokes fluorescence excitation reveals conformational mobility of the C-phycocyanin chromophores Structural Dynamics 9(5):054701 (2022)
Tsoraev G, Protasova E, Klimanova E, Ryzhykau Y, Kuklin A, Semenov Y, Ge B, Li W, Qin S, Friedrich T, Sluchanko N, Maksimov E

R_g^Guinier	3.9	nm
D_max	13.2	nm
Volume^Porod	154	nm³

SASDBV9 – Immunoglobulin domain 4 of Nucleoporin Pom152 (Pom152 Ig-4: amino acids 718-820)

Nucleoporin POM152 experimental SAS data

Sample:	Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae protein
Buffer:	10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment:	SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12

Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J

R_g^Guinier	1.8	nm
D_max	6.7	nm
Volume^Porod	18	nm³

SASDPB4 – SAXS data for the C-phycocyanin in 8 M urea solution

Sample:	C-phycocyanin alpha subunit monomer, 18 kDa Arthrospira platensis protein C-phycocyanin beta subunit monomer, 18 kDa Arthrospira platensis protein
Buffer:	8 M urea, 30 mM βME, pH: 7
Experiment:	SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2022 Apr 14

R_g^Guinier	6.6	nm
D_max	23.5	nm

SASDBW9 – Immunoglobulin domains 4,5 of Nucleoporin Pom152 (Pom152 Ig-4,5: amino acids 718-920)

Sample:	Nucleoporin POM152 monomer, 24 kDa Saccharomyces cerevisiae protein
Buffer:	10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment:	SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12

Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J

R_g^Guinier	2.7	nm
D_max	9.4	nm
Volume^Porod	23	nm³

SASDFT4 – Conformation of the R11-15 human dystrophin fragment (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data

Sample:	Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1

How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O

R_g^Guinier	6.2	nm
D_max	27.4	nm
Volume^Porod	146	nm³

SASDBX9 – Immunoglobulin domain 6 of Nucleoporin Pom152 (Pom152 Ig-6: amino acids 919-1020)

Sample:	Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae protein
Buffer:	10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment:	SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12

Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J

R_g^Guinier	2.8	nm
D_max	7.9	nm
Volume^Porod	57	nm³

SASDFU4 – Conformation of R11-15 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

Sample:	Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1

R_g^Guinier	6.2	nm
D_max	28.1	nm
Volume^Porod	144	nm³

SASDBY9 – Immunoglobulin domains 3,4 of Nucleoporin Pom152 (Pom152 Ig-3,4: amino acids 603-820)

Sample:	Nucleoporin POM152 monomer, 26 kDa Saccharomyces cerevisiae protein
Buffer:	10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment:	SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12

Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J

R_g^Guinier	3.0	nm
D_max	10.5	nm
Volume^Porod	28	nm³

SASDBZ9 – Immunoglobulin domains 4,5,6,7 of Nucleoporin Pom152 (Pom152 Ig-4,5,6,7: amino acids 718-1148)

Sample:	Nucleoporin POM152 monomer, 49 kDa Saccharomyces cerevisiae protein
Buffer:	10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment:	SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12

Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J

R_g^Guinier	4.3	nm
D_max	15.4	nm
Volume^Porod	67	nm³

SASDFV4 – Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Sample:	Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 1

R_g^Guinier	8.1	nm
D_max	29.6	nm
Volume^Porod	231	nm³

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