SASBDB entries for UniProt ID:

SASDKH9 – Mothers against decapentaplegic homolog 4, SMAD4, MH1 fragment (amino acids 10-140)

UniProt ID: Q13485 (10-140) Mothers against decapentaplegic homolog 4 (MH1 fragment)

Mothers against decapentaplegic homolog 4 (MH1 fragment) experimental SAS data
Mothers against decapentaplegic homolog 4 (MH1 fragment) Kratky plot
Sample: Mothers against decapentaplegic homolog 4 (MH1 fragment) monomer, 15 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2015 Apr 20
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 1.6 nm
Dmax 6.0 nm
VolumePorod 24 nm3

SASDKJ9 – C2AB construct of synaptotagmin-1 (SYT1)

UniProt ID: Q9SKR2 (253-541) Synaptotagmin-1

Synaptotagmin-1 experimental SAS data
DAMFILT model
Sample: Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Feb 16
The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites Life Science Alliance 4(10):e202101152 (2021)
Benavente J, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-López N, Botella M, Sánchez-Barrena M, Albert A
RgGuinier 2.8 nm
Dmax 12.6 nm
VolumePorod 50 nm3

SASDKK9 – C2AB construct of synaptotagmin-1 (SYT1) in presence of Ca cations

UniProt ID: Q9SKR2 (253-541) Synaptotagmin-1

Synaptotagmin-1 experimental SAS data
MULTIFOXS model
Sample: Synaptotagmin-1 monomer, 33 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Feb 16
The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites Life Science Alliance 4(10):e202101152 (2021)
Benavente J, Siliqi D, Infantes L, Lagartera L, Mills A, Gago F, Ruiz-López N, Botella M, Sánchez-Barrena M, Albert A
RgGuinier 2.9 nm
Dmax 13.8 nm
VolumePorod 54 nm3

SASDKL9 – Lymphostatin pH7.5

UniProt ID: B7UI23 (1-3223) Efa1/LifA protein

Efa1/LifA protein experimental SAS data
DAMFILT model
Sample: Efa1/LifA protein monomer, 367 kDa Escherichia coli O127:H6 … protein
Buffer: 50 mM Bis-Tris, 100 mM NaCl, 3 % (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 29
Activity of lymphostatin, a lymphocyte inhibitory virulence factor of pathogenic Escherichia coli, is dependent on a cysteine protease motif. J Mol Biol :167200 (2021)
Bease AG, Blackburn EA, Chintoan-Uta C, Webb S, Cassady-Cain RL, Stevens MP
RgGuinier 5.9 nm
Dmax 19.3 nm
VolumePorod 559 nm3

SASDKM9 – Lymphostatin pH5.5

UniProt ID: B7UI23 (1-3223) Efa1/LifA protein

Efa1/LifA protein experimental SAS data
DAMFILT model
Sample: Efa1/LifA protein monomer, 367 kDa Escherichia coli O127:H6 … protein
Buffer: 50 mM Bis-Tris, 100 mM NaCl, 3 % (v/v) glycerol, pH: 5.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 29
Activity of lymphostatin, a lymphocyte inhibitory virulence factor of pathogenic Escherichia coli, is dependent on a cysteine protease motif. J Mol Biol :167200 (2021)
Bease AG, Blackburn EA, Chintoan-Uta C, Webb S, Cassady-Cain RL, Stevens MP
RgGuinier 5.9 nm
Dmax 19.7 nm
VolumePorod 565 nm3

SASDKN9 – Lymphostatin C1480A mutant pH 7.5

UniProt ID: B7UI23 (1-3223) Efa1/LifA protein (C1480A mutant)

Efa1/LifA protein (C1480A mutant) experimental SAS data
DAMMIF model
Sample: Efa1/LifA protein (C1480A mutant) monomer, 367 kDa Escherichia coli O127:H6 … protein
Buffer: 50 mM Bis-Tris, 100 mM NaCl, 3 % (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 29
Activity of lymphostatin, a lymphocyte inhibitory virulence factor of pathogenic Escherichia coli, is dependent on a cysteine protease motif. J Mol Biol :167200 (2021)
Bease AG, Blackburn EA, Chintoan-Uta C, Webb S, Cassady-Cain RL, Stevens MP
RgGuinier 5.9 nm
Dmax 19.1 nm
VolumePorod 557 nm3

SASDKP9 – Lymphostatin C1480A mutant pH5.5

UniProt ID: B7UI23 (1-3223) Efa1/LifA protein (C1480A mutant)

Efa1/LifA protein (C1480A mutant) experimental SAS data
DAMFILT model
Sample: Efa1/LifA protein (C1480A mutant) monomer, 367 kDa Escherichia coli O127:H6 … protein
Buffer: 50 mM Bis-Tris, 100 mM NaCl, 3 % (v/v) glycerol, pH: 5.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 29
Activity of lymphostatin, a lymphocyte inhibitory virulence factor of pathogenic Escherichia coli, is dependent on a cysteine protease motif. J Mol Biol :167200 (2021)
Bease AG, Blackburn EA, Chintoan-Uta C, Webb S, Cassady-Cain RL, Stevens MP
RgGuinier 5.8 nm
Dmax 19.3 nm
VolumePorod 560 nm3

SASDKQ9 – Chaperone protein IpgC, symmetric dimer from Shigella flexneri

UniProt ID: P0A2U4 (2-155) Chaperone protein IpgC

Chaperone protein IpgC experimental SAS data
CORAL model
Sample: Chaperone protein IpgC dimer, 39 kDa Shigella flexneri protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2012 Dec 10
Structural Insights of Shigella Translocator IpaB and Its Chaperone IpgC in Solution Frontiers in Cellular and Infection Microbiology 11 (2021)
Ferrari M, Charova S, Sansonetti P, Mylonas E, Gazi A
RgGuinier 2.7 nm
Dmax 9.0 nm
VolumePorod 56 nm3

SASDKR9 – The chaperone protein IpgC/invasin IpaB heterodimer complex from Shigella flexneri

UniProt ID: P0A2U4 (2-155) T3SS Chaperone protein IpgC

UniProt ID: P18011 (1-580) Invasin IpaB

T3SS Chaperone protein IpgCInvasin IpaB experimental SAS data
EOM/RANCH model
Sample: T3SS Chaperone protein IpgC monomer, 20 kDa Shigella flexneri protein
Invasin IpaB monomer, 62 kDa Shigella flexneri protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2012 Dec 10
Structural Insights of Shigella Translocator IpaB and Its Chaperone IpgC in Solution Frontiers in Cellular and Infection Microbiology 11 (2021)
Ferrari M, Charova S, Sansonetti P, Mylonas E, Gazi A
RgGuinier 3.9 nm
Dmax 14.0 nm
VolumePorod 165 nm3

SASDKT9 – The Moco-free form of the Moco carrier protein from Rippkaea orientalis

UniProt ID: B7K4Z0 (1-163) p450 cytochrome, putative (Moco carrier protein)

p450 cytochrome, putative (Moco carrier protein) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: P450 cytochrome, putative (Moco carrier protein) tetramer, 75 kDa Rippkaea orientalis (strain … protein
Buffer: 100 mM Tris-HCl, 300 mM NaCl, 2 %(v/v) glycerol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Feb 5
The structure of the Moco carrier protein from Rippkaea orientalis. Acta Crystallogr F Struct Biol Commun 76(Pt 9):453-463 (2020)
Krausze J, Hercher TW, Archna A, Kruse T
RgGuinier 2.8 nm
Dmax 8.5 nm
VolumePorod 107 nm3