SAXS data for Chitin-binding protein (CbpD) from Pseudomonas aeruginosa

Henrik Vinther Sørensen.

SASDK42 – Chitin-binding protein CbpD (Pseudomonas aeruginosa), ESRF BM29 data

Chitin-binding protein CbpD
MWI(0) 39 kDa
MWexpected 39 kDa
VPorod 64131 nm3
log I(s) 3.08×10-2 3.08×10-3 3.08×10-4 3.08×10-5
Chitin-binding protein CbpD small angle scattering data  s, nm-1
ln I(s)
Chitin-binding protein CbpD Guinier plot ln 3.08×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Chitin-binding protein CbpD Kratky plot 1.104 0 3 sRg
p(r)
Chitin-binding protein CbpD pair distance distribution function Rg: 3.4 nm 0 Dmax: 12 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Chitin-binding protein CbpD DAMMIN model

log I(s)
 s, nm-1
Chitin-binding protein CbpD OTHER model

log I(s)
 s, nm-1
Chitin-binding protein CbpD DAMMIF model

Synchrotron SAXS data from solutions of Chitin-binding protein CbpD (Pseudomonas aeruginosa), ESRF BM29 data in 15 mM Tris-HCl 150 mM NaCl, pH 7.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.991862 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.3 and 2.5 mg/ml were measured at 20°C. 10 successive 1 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

CbpD was measured at four concentration: 2.50, 1.25, 0.63, 0.31 mg/mL at 20 °C at ESRF BM29. Data extrapolated to infinite dilution and scaled to 1 mg/mL.

Chitin-binding protein CbpD (CbpD)
Mol. type   Protein
Organism   Pseudomonas aeruginosa
Olig. state   Monomer
Mon. MW   39.2 kDa
 
UniProt   Q9I589 (26-389)
Sequence   FASTA