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32 hits found for Andrew Whitten

SASDHE2 – Type 1 insulin-like growth factor receptor ectodomains (IGF-1RΔβ)

Insulin-like growth factor 1 receptor experimental SAS data
BUNCH model
Sample: Insulin-like growth factor 1 receptor dimer, 202 kDa Homo sapiens protein
Buffer: 30 mM Tris, 140 mM NaCl, 0.02% w/v sodium azide,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2008 Apr 22
Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformat... J Mol Biol 394(5):878-92 (2009)
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC
RgGuinier 5.1 nm
Dmax 16.0 nm
VolumePorod 357 nm3

SASDHF2 – Insulin receptor ectodomains (IRΔβ)

Insulin receptor experimental SAS data
BUNCH model
Sample: Insulin receptor dimer, 203 kDa Homo sapiens protein
Buffer: 30 mM Tris, 140 mM NaCl, 0.02% w/v sodium azide,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2008 Dec 7
Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformat... J Mol Biol 394(5):878-92 (2009)
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC
RgGuinier 5.5 nm
Dmax 17.0 nm
VolumePorod 385 nm3

SASDHY2 – Human APPL2 (DCC-interacting protein 13-beta)

Adaptor protein, phosphotyrosine interaction, pleckstrin homology domain, and leucine zipper-containing protein 2 experimental SAS data
BUNCH model
Sample: Adaptor protein, phosphotyrosine interaction, pleckstrin homology domain, and leucine zipper-containing protein 2 dimer, 87 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 7 Apr 20
Membrane curvature protein exhibits interdomain flexibility and binds a small GTPase. J Biol Chem 287(49):40996-1006 (2012)
...Whitten AE, Martin JL
RgGuinier 5.1 nm
Dmax 18.0 nm
VolumePorod 140 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
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
...Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 92 nm3

SASDH23 – Antigen 43 alpha domain

Alpha domain of Ag43a experimental SAS data
DAMMIN model
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2009 Nov 19
The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping. Proc Natl Acad Sci U S A 111(1):457-62 (2014)
...Whitten AE, Schembri MA
RgGuinier 3.6 nm
Dmax 12.2 nm
VolumePorod 62 nm3

SASDF33 – Antigen 43/Fragment antigen-binding region Fab10C12 complex (Ag43-Fab)

Alpha domain of Ag43aFragment antigen-binding region Fab10C12 experimental SAS data
DAMFILT model
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Fragment antigen-binding region Fab10C12 monomer, 47 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Nov 3
Inhibition of aggregation and biofilm formation by Uropathogenic Escherichia coli
Andrew Whitten
RgGuinier 4.3 nm
Dmax 15.0 nm
VolumePorod 103 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
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
...Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 88 nm3

SASDH43 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
...Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.2 nm
Dmax 10.0 nm
VolumePorod 135 nm3

SASDH53 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with calcium

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
...Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 160 nm3

SASDH63 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, 0.25 mM IP3, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
...Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.1 nm
Dmax 8.8 nm
VolumePorod 115 nm3

SASDH73 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3) plus calcium

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, 0.25 mM IP3, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
...Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.2 nm
Dmax 9.6 nm
VolumePorod 132 nm3

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
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
...Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 195 nm3

SASDKP3 – Alpha domain of autotransporter adhesin Ag43a from Escherichia coli strain UTI89 / UPEC (alpha-Ag43_UTI)

Putative autotransporter experimental SAS data
Sample: Putative autotransporter dimer, 119 kDa Escherichia coli (strain … protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 May 1
Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms npj Biofilms and Microbiomes 8(1) (2022)
...Whitten A, Hor L, Peters K, Ageorges V, Caccia N, Desvaux M, Schembri M, Paxman J, Heras B
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 79 nm3

SASDKQ3 – Alpha domain of autotransporter adhesin Ag43a from Escherichia coli

Alpha domain of Ag43a experimental SAS data
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Nov 3
Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms npj Biofilms and Microbiomes 8(1) (2022)
...Whitten A, Hor L, Peters K, Ageorges V, Caccia N, Desvaux M, Schembri M, Paxman J, Heras B
RgGuinier 4.6 nm
Dmax 18.0 nm
VolumePorod 87 nm3

SASDHY3 – KinA-Sda complex

Sporulation kinase ASporulation inhibitor sda experimental SAS data
SASREF model
Sample: Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Sporulation inhibitor sda dimer, 11 kDa Bacillus subtilis protein
Buffer: 50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Nov 16
The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB
RgGuinier 2.9 nm
Dmax 8.0 nm
VolumePorod 85 nm3

SASDHZ3 – Sporulation kinase A

Sporulation kinase A experimental SAS data
SASREF model
Sample: Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Buffer: 50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Mar 18
The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB
RgGuinier 2.9 nm
Dmax 9.5 nm
VolumePorod 76 nm3

SASDB94 – Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data
Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis Rg histogram
Sample: C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer: 25 mM HEPES 150mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Nat Commun 8:16065 (2017)
...Whitten AE, Choudhury HG, Schembri MA, Martin JL
RgGuinier 3.7 nm
Dmax 10.5 nm
VolumePorod 92 nm3

SASDC45 – Alpha domain of autotransporter protein UpaB from UPEC

Alpha domain of autotransporter protein UpaB experimental SAS data
CORAL model
Sample: Alpha domain of autotransporter protein UpaB monomer, 48 kDa E. Coli CFT073 protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 May 1
Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules. Nat Commun 10(1):1967 (2019)
...Whitten AE, Wang G, Luan CH, Moriel DG, Tan L, Peters KM, Phan MD, Gee CL, Ulett GC, Schembri MA, Heras B
RgGuinier 2.9 nm
Dmax 10.5 nm
VolumePorod 66 nm3

SASDJ85 – Zinc transporter 1 – hZnT1-CTD

Zinc transporter 1 experimental SAS data
DAMFILT model
Sample: Zinc transporter 1 dimer, 37 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, pH: 7.6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 14
Heterologous Expression and Biochemical Characterization of the Human Zinc Transporter 1 (ZnT1) and Its Soluble C-Terminal Domain Frontiers in Chemistry 9 (2021)
...Whitten A, Choudhury H, Drew D, Martin J
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 50 nm3

SASDBW6 – Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant)

Suppressor of Copper Sensitivity C protein (mutant) experimental SAS data
Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant) Rg histogram
Sample: Suppressor of Copper Sensitivity C protein (mutant) trimer, 73 kDa Proteus mirabilis protein
Buffer: 25 mM HEPES 150mM NaCl, 1mM DTT,, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Jul 22
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Nat Commun 8:16065 (2017)
...Whitten AE, Choudhury HG, Schembri MA, Martin JL
RgGuinier 4.4 nm
Dmax 13.5 nm
VolumePorod 108 nm3

SASDCH7 – N-terminal domain of DsbD from N. meningitidis

N-terminus of disulfide interchange protein DsbD experimental SAS data
DAMMIN model
Sample: N-terminus of disulfide interchange protein DsbD monomer, 14 kDa Neisseria meningitidis protein
Buffer: 25mM HEPES 150mM NaCl, pH: 6.7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2013 May 4
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis. Acta Crystallogr F Struct Biol Commun 74(Pt 1):31-38 (2018)
...Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B
RgGuinier 1.8 nm
Dmax 5.7 nm
VolumePorod 17 nm3

SASDCJ7 – C-terminal domain of DsbD from N. meningitidis

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) monomer, 21 kDa Wolbachia endosymbiont of … protein
Buffer: 25mM HEPES 150mM NaCl, pH: 6.7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2013 May 4
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis. Acta Crystallogr F Struct Biol Commun 74(Pt 1):31-38 (2018)
...Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B
RgGuinier 1.5 nm
Dmax 4.5 nm
VolumePorod 15 nm3

SASDJL7 – Oxidised fimbrial BcfH protein

Hypothetical exported protein experimental SAS data
CORAL model
Sample: Hypothetical exported protein trimer, 83 kDa Salmonella typhimurium (strain … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 14
Salmonella enterica BcfH is a trimeric thioredoxin-like bifunctional enzyme with both thiol oxidase and disulfide isomerase activities. Antioxid Redox Signal (2021)
...Whitten AE, Panjikar S, Santos-Martin CF, Martin JL, Totsika M, Heras B
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 93 nm3

SASDC28 – Mature α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) trimer, 81 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2014 Mar 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
...Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 2.8 nm
Dmax 8.7 nm
VolumePorod 913 nm3

SASDC38 – Truncated α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) monomer, 21 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
...Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 1.9 nm
Dmax 6.3 nm
VolumePorod 275 nm3

SASDC48 – ScsC-ScsBalpha complex

DsbA-like proteinPutative metal resistance protein experimental SAS data
SASREF model
Sample: DsbA-like protein trimer, 74 kDa Proteus mirabilis protein
Putative metal resistance protein monomer, 30 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Nov 2
Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB. J Biol Chem 293(16):5793-5805 (2018)
...Whitten AE, Martin JL
RgGuinier 3.9 nm
Dmax 11.5 nm
VolumePorod 145 nm3

SASDMG8 – Splicing factor, proline- and glutamine-rich-QM bound to Non-POU domain-containing octamer-binding protein: SFPQ(276-598)-QM / NONO(53-312) heterodimer

Non-POU domain-containing octamer-binding proteinSplicing factor, proline- and glutamine-rich experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Non-POU domain-containing octamer-binding protein monomer, 30 kDa Homo sapiens protein
Splicing factor, proline- and glutamine-rich monomer, 38 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ Nucleic Acids Research 48(6):3356-3365 (2020)
...Whitten A, Caria S, Lim Y, Badhan R, Anggono V, Lee M
RgGuinier 4.0 nm
Dmax 16.5 nm
VolumePorod 90 nm3

SASDMH8 – Splicing factor, proline- and glutamine-rich-QM-TM bound to Non-POU domain-containing octamer-binding protein: SFPQ(276-598)-QM-TM / NONO(52-312) heterodimer

Splicing factor, proline- and glutamine-richNon-POU domain-containing octamer-binding protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Splicing factor, proline- and glutamine-rich monomer, 38 kDa Homo sapiens protein
Non-POU domain-containing octamer-binding protein monomer, 30 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Nov 8
Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ Nucleic Acids Research 48(6):3356-3365 (2020)
...Whitten A, Caria S, Lim Y, Badhan R, Anggono V, Lee M
RgGuinier 3.6 nm
Dmax 16.5 nm
VolumePorod 80 nm3

SASDLE9 – Suppressor of Copper Sensitivity C protein from Caulobacter crescentus

Thioredoxin domain-containing protein experimental SAS data
Suppressor of Copper Sensitivity C protein from Caulobacter crescentus Rg histogram
Sample: Thioredoxin domain-containing protein trimer, 73 kDa Caulobacter vibrioides (strain … protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 21
The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity Acta Crystallographica Section D Structural Biology 78(3):337-352 (2022)
...Whitten A, Furlong E, McCoy A, Gulbis J, Totsika M, Martin J, Halili M
RgGuinier 3.9 nm
Dmax 12.0 nm
VolumePorod 97 nm3

SASDEK4 – C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC)

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data
DAMFILT model
Sample: C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
...Whitten AE, Martin JL
RgGuinier 1.7 nm
Dmax 5.4 nm
VolumePorod 22200 nm3

SASDER4 – Wild-type suppressor of copper sensitivity C protein, PmScsC, with concentration series data

Suppressor of Copper Sensitivity C protein experimental SAS data
OTHER model
Sample: Suppressor of Copper Sensitivity C protein trimer, 74 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
...Whitten AE, Martin JL
RgGuinier 3.7 nm
Dmax 11.1 nm
VolumePorod 101 nm3

SASDEQ4 – Deletion mutant of the suppressor of copper sensitivity C protein, PmScsC, with concentration series data

Deletion mutant of PmScsC experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Deletion mutant of PmScsC , 23 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 5
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis. Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019)
...Whitten AE, Martin JL
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 54 nm3