Browse by MACROMOLECULE type: protein

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

SASDBR2 – Contactin-associated protein-like 2 (Caspr2) extracellular domains 1-1261.

Contactin-associated protein-like 2 extracellular domains (1-1261) experimental SAS data
DAMMIN model
Sample: Contactin-associated protein-like 2 extracellular domains (1-1261) monomer, 140 kDa Homo sapiens protein
Buffer: 10 mM HEPES 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2010 Oct 4
Structural Characterization of the Extracellular Domain of CASPR2 and Insights into Its Association with the Novel Ligand Contactin1. J Biol Chem 291(11):5788-802 (2016)
Rubio-Marrero EN, Vincelli G, Jeffries CM, Shaikh TR, Pakos IS, Ranaivoson FM, von Daake S, Demeler B, De Jaco A, Perkins G, Ellisman MH, Trewhella J, Comoletti D
RgGuinier 4.4 nm
Dmax 14.5 nm
VolumePorod 282 nm3

SASDAX8 – Ribokinase ThiM

Ribokinase ThiM experimental SAS data
CORAL model
Sample: Ribokinase ThiM trimer, 89 kDa Staphylococcus aureus protein
Buffer: 50 mM Potassium phosphate 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 19
Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections. Sci Rep 6:22871 (2016)
Drebes J, Künz M, Windshügel B, Kikhney AG, Müller IB, Eberle RJ, Oberthür D, Cang H, Svergun DI, Perbandt M, Betzel C, Wrenger C
RgGuinier 3.0 nm
Dmax 9.0 nm
VolumePorod 145 nm3

SASDAD7 – Structure of a complex between full length and truncated CTP1L endolysin

Endolysin  experimental SAS data
CRYSOL model
Sample: Endolysin , 33 kDa Clostridium phage phiCTP1 protein
Buffer: 20 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17
Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product. J Biol Chem 291(10):4882-93 (2016)
Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gómez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R
RgGuinier 3.7 nm
Dmax 13.8 nm
VolumePorod 95 nm3

SASDAE7 – Structure of a complex between full length and truncated CS74L endolysin

Endolysin CS74L  experimental SAS data
DAMMIF model
Sample: Endolysin CS74L , 31 kDa Clostridium phage phi8074-B1 protein
Buffer: 20 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17
Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product. J Biol Chem 291(10):4882-93 (2016)
Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gómez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R
RgGuinier 3.6 nm
Dmax 14.0 nm
VolumePorod 79 nm3