SAXS/WAXS data of conformationally flexible ribose binding protein

Choudhury J, Yonezawa K, Anu A, Shimizu N, Chaudhuri B, Data in Brief :109932 (2023) DOI

SASDSE9 – SAXS data of poly-histidine tagged Ribose Binding Protein (9 mg/mL) from Escherichia coli in the presence of 1 mM ribose

Ribose import binding protein RbsB
Ribose
MWexperimental 21 kDa
MWexpected 30 kDa
VPorod 35 nm3
log I(s) 5.13×101 5.13×100 5.13×10-1 5.13×10-2
Ribose import binding protein RbsB Ribose small angle scattering data  s, nm-1
ln I(s)
Ribose import binding protein RbsB Ribose Guinier plot ln 5.14×101 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Ribose import binding protein RbsB Ribose Kratky plot 1.104 0 3 sRg
p(r)
Ribose import binding protein RbsB Ribose pair distance distribution function Rg: 2.1 nm 0 Dmax: 8.3 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of poly-histidine tagged Ribose Binding Protein in 50 mM Tris, 50 mM NaCl, 10% glycerol, 1 mM ribose, pH 7 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 9.00 mg/ml was measured at 4°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.

Ribose import binding protein RbsB
Mol. type   Protein
Organism   Escherichia coli (strain K12)
Olig. state   Monomer
Mon. MW   29.7 kDa
 
UniProt   P02925 (25-296)
Sequence   FASTA
 
Ribose
Mol. type   Other
Olig. state   Monomer
Mon. MW   0.2 kDa
Chemical formula