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

SASDA68 – Aldolase in Tris/HCl

Fructose-bisphosphate aldolase A
MWI(0) 155 kDa
MWexpected 157 kDa
log I(s) 3.89×102 3.89×101 3.89×100 3.89×10-1
Fructose-bisphosphate aldolase A small angle scattering data  s, nm-1
ln I(s)
Fructose-bisphosphate aldolase A Guinier plot ln 3.89×102 Rg: 3.6 nm 0 (3.6 nm)-2 s2
Fructose-bisphosphate aldolase A Kratky plot 1.104 0 3 sRg
Fructose-bisphosphate aldolase A pair distance distribution function Rg: 3.6 nm 0 Dmax: 10.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Fructose-bisphosphate aldolase A PDB (PROTEIN DATA BANK) model

Synchrotron SAXS data from solutions of Aldolase 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 4.90 mg/ml was measured at 20°C. Eight successive 15 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. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

Tags: benchmark X33
Fructose-bisphosphate aldolase A
Mol. type   Protein
Organism   Oryctolagus cuniculus
Olig. state   Tetramer
Mon. MW   39.3 kDa
UniProt   P00883 (2-364)
Sequence   FASTA