Browse by MACROMOLECULE type: protein

SASDAN2 – Bovine pancreatic ribonuclease A in PBS (WAXS)

Ribonuclease pancreatic experimental SAS data
GASBOR model
Sample: Ribonuclease pancreatic monomer, 16 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 18
Standard proteins
Darja Ruskule
RgGuinier 1.6 nm
Dmax 5.0 nm
VolumePorod 15 nm3

SASDAQ2 – Ubiquitin in sodium acetate

Ubiquitin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ubiquitin monomer, 9 kDa Bos taurus protein
Buffer: 40 mM Sodium acetate 150 mM NaCl, pH: 5.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 18
Standard proteins
Darja Ruskule
RgGuinier 1.3 nm
Dmax 4.9 nm
VolumePorod 12 nm3

SASDAR2 – Bovine pancreatic ribonuclease A in PBS

Ribonuclease pancreatic experimental SAS data
DAMMIF model
Sample: Ribonuclease pancreatic monomer, 16 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 18
Standard proteins
Darja Ruskule
RgGuinier 1.6 nm
Dmax 5.0 nm
VolumePorod 17 nm3

SASDAK6 – Glucose Isomerase

Xylose isomerase experimental SAS data
DAMMIF model
Sample: Xylose isomerase tetramer, 172 kDa Streptomyces rubiginosus protein
Buffer: PBS, 50% Glycerol, 0.076 M NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Apr 24
Standard proteins
Erica Valentini
RgGuinier 3.4 nm
Dmax 9.7 nm
VolumePorod 293 nm3

SASDAB8 – Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).

PRKCA-binding protein experimental SAS data
Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition). Rg histogram
Sample: PRKCA-binding protein dimer, 93 kDa Rattus norvegicus protein
Buffer: 50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2015 May 11
Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering. Structure 23(7):1258-1270 (2015)
Karlsen ML, Thorsen TS, Johner N, Ammendrup-Johnsen I, Erlendsson S, Tian X, Simonsen JB, Høiberg-Nielsen R, Christensen NM, Khelashvili G, Streicher W, Teilum K, Vestergaard B, Weinstein H, Gether U, Arleth L, Madsen KL
RgGuinier 6.0 nm
Dmax 20.0 nm
VolumePorod 205 nm3

SASDA58 – UL26N of pseudorabies virus

VP24 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: VP24 dimer, 53 kDa Suid herpesvirus 1 protein
Buffer: 50 mM Tris/HCl 0.5 M NaCl 0.25 M imidazole 5% glycerol 50 mM urea 0.2 M MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine Protease. PLoS Pathog 11(7):e1005045 (2015)
Zühlsdorf M, Werten S, Klupp BG, Palm GJ, Mettenleiter TC, Hinrichs W
RgGuinier 2.6 nm
Dmax 10.6 nm
VolumePorod 73 nm3

SASDCL6 – Lys63-linked dimer ubiquitin

Polyubiquitin-C experimental SAS data
Polyubiquitin-C Kratky plot
Sample: Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Buffer: 100mM NaCl, 10mM sodium acetate, pH: 6
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Mar 24
Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition. Elife 4 (2015)
Liu Z, Gong Z, Jiang WX, Yang J, Zhu WK, Guo DC, Zhang WP, Liu ML, Tang C
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 24 nm3

SASDAS7 – mouse olfactomedin-1

Noelin experimental SAS data
DAMMIF model
Sample: Noelin tetramer, 256 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 6
Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure. J Biol Chem 290(24):15092-101 (2015)
Pronker MF, Bos TG, Sharp TH, Thies-Weesie DM, Janssen BJ
RgGuinier 8.5 nm
Dmax 30.0 nm
VolumePorod 616 nm3

SASDA37 – Surface Protein G (SasG) EG5 repeat protein G51-G52

Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 24 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 4.7 nm
Dmax 19.0 nm
VolumePorod 29 nm3

SASDA47 – Surface Protein G (SasG) EG5 repeat protein G51-G53

Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 39 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 7.7 nm
Dmax 30.5 nm
VolumePorod 49 nm3