SASBDB entries for UniProt ID:

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

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4

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
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with 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

SASDGM5 – Holo-RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA)

UniProt ID: P0DKX7 (1007-1706) RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA)

RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) experimental SAS data
OTHER model
Sample: RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) monomer, 73 kDa Bordetella pertussis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM DTT, 4 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 May 31
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion. Sci Rep 5:14223 (2015)
O'Brien DP, Hernandez B, Durand D, Hourdel V, Sotomayor-Pérez AC, Vachette P, Ghomi M, Chamot-Rooke J, Ladant D, Brier S, Chenal A
RgGuinier 4.4 nm
Dmax 15.5 nm
VolumePorod 89 nm3

SASDGN5 – apo-RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA)

UniProt ID: P0DKX7 (1007-1706) RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA)

RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) experimental SAS data
OTHER model
Sample: RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) monomer, 73 kDa Bordetella pertussis protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 May 31
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion. Sci Rep 5:14223 (2015)
O'Brien DP, Hernandez B, Durand D, Hourdel V, Sotomayor-Pérez AC, Vachette P, Ghomi M, Chamot-Rooke J, Ladant D, Brier S, Chenal A
RgGuinier 8.3 nm
Dmax 33.0 nm

SASDGP5 – Vibrio cholerae DciA

UniProt ID: Q9KPH3 (1-157) DciA

DciA experimental SAS data
DciA Kratky plot
Sample: DciA monomer, 18 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Mar 26
Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. Nucleic Acids Res (2021)
Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Cheruel S, Ferat JL
RgGuinier 2.7 nm
Dmax 10.1 nm
VolumePorod 26 nm3

SASDGQ5 – Vibrio cholerae hexameric DnaB helicase with bound ATP (VcDnaB.ATP)

UniProt ID: A0A0H3AIB6 (1-468) Replicative DNA helicase (DnaB)

Replicative DNA helicase (DnaB) experimental SAS data
Replicative DNA helicase (DnaB) Kratky plot
Sample: Replicative DNA helicase (DnaB) hexamer, 317 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 1 mM ATP, pH: 8.8
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Oct 4
Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. Nucleic Acids Res (2021)
Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Cheruel S, Ferat JL
RgGuinier 4.6 nm
Dmax 13.0 nm
VolumePorod 585 nm3

SASDGR5 – The Vibrio cholerae DciA/DnaB helicase complex in the presence of bound ATP (VcDnaB.DciA.ATP)

UniProt ID: A0A0H3AIB6 (1-468) DnaB helicase complexed with ATP

UniProt ID: Q9KPH3 (1-157) DciA

DnaB helicase complexed with ATPDciA experimental SAS data
DnaB helicase complexed with ATP DciA Kratky plot
Sample: DnaB helicase complexed with ATP hexamer, 317 kDa Vibrio cholerae serotype … protein
DciA, 55 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 1 mM ATP, pH: 8.8
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Oct 4
Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. Nucleic Acids Res (2021)
Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Cheruel S, Ferat JL
RgGuinier 5.0 nm
Dmax 15.6 nm
VolumePorod 670 nm3

SASDGS5 – MvaT (low salt data set)

UniProt ID: Q9HW86 (1-124) MvaT(mutant)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 50 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.6 nm
Dmax 14.7 nm
VolumePorod 47 nm3

SASDGT5 – MvaT (high salt data set)

UniProt ID: Q9HW86 (1-124) MvaT(mutant)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 300 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.8 nm
Dmax 15.8 nm
VolumePorod 50 nm3

SASDGU5 – The C-terminal cell-surface signaling domain of the Pseudomonas capeferrum anti-sigma regulator PupR in complex with the outer membrane transporter PupB N-terminal signaling domain

UniProt ID: Q52209 (110-324) PupR protein

UniProt ID: P38047 (None-None) Ferric-pseudobactin BN7/BN8 receptor

PupR proteinFerric-pseudobactin BN7/BN8 receptor experimental SAS data
DAMFILT model
Sample: PupR protein monomer, 24 kDa Pseudomonas putida protein
Ferric-pseudobactin BN7/BN8 receptor monomer, 8 kDa Pseudomonas putida protein
Buffer: 25 mM HEPES 400 mM LiCl 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Mar 16
Structural basis of cell surface signaling by a conserved sigma regulator in Gram-negative bacteria. J Biol Chem (2020)
Jensen JL, Jernberg BD, Sinha S, Colbert CL
RgGuinier 2.5 nm
Dmax 8.7 nm
VolumePorod 56 nm3

SASDGV5 – The nucleotide binding domain of Lipid A export ATP-binding/permease protein MsbA - data from stop-and-flow time-resolved SAXS (12 s time course)

UniProt ID: P60752 (338-582) Lipid A export ATP-binding/permease protein MsbA - Nucleotide binding domain

Lipid A export ATP-binding/permease protein MsbA - Nucleotide binding domain experimental SAS data
Lipid A export ATP-binding/permease protein MsbA - Nucleotide binding domain Kratky plot
Sample: Lipid A export ATP-binding/permease protein MsbA - Nucleotide binding domain monomer, 27 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 5 mM MgCl2, 0.45 mM Mg2+-ATP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Dec 8
Structural Kinetics of MsbA Investigated by Stopped-Flow Time-Resolved Small-Angle X-Ray Scattering. Structure (2019)
Josts I, Gao Y, Monteiro DCF, Niebling S, Nitsche J, Veith K, Gräwert TW, Blanchet CE, Schroer MA, Huse N, Pearson AR, Svergun DI, Tidow H
RgGuinier 2.1 nm
Dmax 6.8 nm
VolumePorod 50 nm3