The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces.

Wong E, Vaaje-Kolstad G, Ghosh A, Hurtado-Guerrero R, Konarev PV, Ibrahim AF, Svergun DI, Eijsink VG, Chatterjee NS, van Aalten DM, PLoS Pathog 8(1):e1002373 (2012) Europe PMC

SASDAA4 – Full length GbpA

Full length GbpA
MWexperimental 60 kDa
MWexpected 54 kDa
VPorod 100 nm3
log I(s) 1.60×102 1.60×101 1.60×100 1.60×10-1
Full length GbpA small angle scattering data  s, nm-1
ln I(s)
Full length GbpA Guinier plot ln 1.60×102 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Full length GbpA Kratky plot 1.104 0 √3 sRg
Dmax: 14.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Full length GbpA GASBOR model
log I(s)
 s, nm-1
Full length GbpA SASREF model
Synchrotron SAXS data from solutions of Full length GbpA in 25 mM Tris/HCl 150 mM NaCl, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 10°C. Two successive 120 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Sample detector distance = UNKNOWN

Tags: X33
Full length GbpA (GbpA_full)
Mol. type   Protein
Organism   Vibrio cholerae
Olig. state   Monomer
Mon. MW   54 kDa
Sequence   FASTA