|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|