Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering

Mylonas E, Svergun D, Journal of Applied Crystallography 40(s1):s245-s249 (2007) DOI

SASDAA8 – Chymotrypsinogen A in Tris/HCl

Chymotrypsinogen A
MWI(0) 26 kDa
MWexpected 26 kDa
log I(s) 8.75×101 8.75×100 8.75×10-1 8.75×10-2
Chymotrypsinogen A small angle scattering data  s, nm-1
ln I(s)
Chymotrypsinogen A Guinier plot ln 8.75×101 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Chymotrypsinogen A Kratky plot 1.104 0 √3 sRg
p(r)
Chymotrypsinogen A pair distance distribution function Rg: 1.7 nm 0 Dmax: 5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Chymotrypsinogen A CRYSOL model
Synchrotron SAXS data from solutions of Chymotrypsinogen A in Tris/HCl in 100 mM Tris/HCl 100 mM NaCl, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III 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 6.02 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Tags: benchmark X33
Chymotrypsinogen A
Mol. type   Protein
Organism   Bos taurus
Olig. state   Monomer
Mon. MW   25.7 kDa
 
UniProt   P00766
Sequence   FASTA