SASDC84 – parDE-like toxin-antitoxin module, EcPaaA2_13-63-HisEcParE2 construct

Plasmid stabilization protein ParEUncharacterized protein experimental SAS data
parDE-like toxin-antitoxin module, EcPaaA2_13-63-HisEcParE2 construct Rg histogram
Sample: Plasmid stabilization protein ParE monomer, 13 kDa Escherichia coli protein
Uncharacterized protein monomer, 6 kDa Escherichia coli O157:H7 protein
Buffer: 50 mM Tris-HCl, 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 Feb 5
A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. J Mol Biol 428(8):1589-603 (2016)
Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R
RgGuinier 2.2 nm
Dmax 9.3 nm
VolumePorod 36 nm3

SASDBT4 – Bovine serum albumin monomer (measured by SEC-SAXS)

Bovine serum albumin, monomer experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Bovine serum albumin, monomer monomer, 66 kDa Bos taurus protein
Buffer: 20 mM Tris 142 mM NaCl 5 % Glycerol 1mM DTT, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 22
Bovine Serum Albumin measured by SEC-SAXS
Martha Brennich
RgGuinier 2.7 nm
Dmax 8.2 nm
VolumePorod 118 nm3

SASDB74 – CyaA Block I-V

Adenylate cyclase toxin Block I-V experimental SAS data
DAMMIF model
Sample: Adenylate cyclase toxin Block I-V monomer, 70 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl 150 mM NaCl 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Mol Cell 62(1):47-62 (2016)
Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P
RgGuinier 5.6 nm
Dmax 17.2 nm
VolumePorod 275 nm3

SASDB84 – CyaA Block V

Adenylate cyclase toxin Block V experimental SAS data
DAMMIF model
Sample: Adenylate cyclase toxin Block V monomer, 16 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl 150 mM NaCl 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Mol Cell 62(1):47-62 (2016)
Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P
RgGuinier 1.8 nm
Dmax 5.9 nm
VolumePorod 24 nm3

SASDBN2 – Human linear diubiquitin

Linear di-ubiquitin experimental SAS data
Human linear diubiquitin Rg histogram
Sample: Linear di-ubiquitin monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
Thach TT, Shin D, Han S, Lee S
RgGuinier 2.1 nm
Dmax 6.6 nm
VolumePorod 20 nm3

SASDBP2 – Human linear triubiquitin

Human linear tri-ubiquitin experimental SAS data
Human linear triubiquitin Rg histogram
Sample: Human linear tri-ubiquitin monomer, 26 kDa Homo sapiens protein
Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
Thach TT, Shin D, Han S, Lee S
RgGuinier 2.5 nm
Dmax 8.6 nm
VolumePorod 36 nm3

SASDBQ2 – Human linear tetraubiquitin

Human linear tetra-ubiquitin experimental SAS data
Human linear tetraubiquitin Rg histogram
Sample: Human linear tetra-ubiquitin monomer, 34 kDa Homo sapiens protein
Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
Thach TT, Shin D, Han S, Lee S
RgGuinier 3.1 nm
Dmax 11.2 nm
VolumePorod 49 nm3

SASDMU4 – Retinoic acid receptor RXR-alpha ligand binding domain (LBD)

Retinoic acid receptor RXR-alpha experimental SAS data
CUSTOM IN-HOUSE model
Sample: Retinoic acid receptor RXR-alpha dimer, 51 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 100 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 2.5 nm
Dmax 8.3 nm
VolumePorod 60 nm3

SASDMV4 – Full-length Retinoic acid receptor RXR-alpha in complex with Ramp2 DNA

Retinoic acid receptor RXR-alphaRamp2 DNA experimental SAS data
EOM/RANCH model
Sample: Retinoic acid receptor RXR-alpha dimer, 102 kDa Homo sapiens protein
Ramp2 DNA monomer, 11 kDa DNA
Buffer: 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 May 7
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 4.4 nm
Dmax 13.9 nm
VolumePorod 161 nm3

SASDMW4 – Retinoic acid receptor RXR-alpha N-terminal and DNA binding domains (DBD) in complex with Ramp2 DNA

Ramp2 DNARetinoic acid receptor RXR-alpha experimental SAS data
EOM/RANCH model
Sample: Ramp2 DNA monomer, 11 kDa DNA
Retinoic acid receptor RXR-alpha dimer, 44 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Jul 17
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 4.3 nm
Dmax 14.3 nm
VolumePorod 89 nm3

4725 hits found.