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

SASDA78 – Carbonic Anhydrase in Tris/HCl

Carbonic anhydrase 2
MWI(0) 33 kDa
MWexpected 29 kDa
log I(s) 1.19×102 1.19×101 1.19×100 1.19×10-1
Carbonic anhydrase 2 small angle scattering data  s, nm-1
ln I(s)
Carbonic anhydrase 2 Guinier plot ln 1.20×102 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Carbonic anhydrase 2 Kratky plot 1.104 0 √3 sRg
p(r)
Carbonic anhydrase 2 pair distance distribution function Rg: 1.9 nm 0 Dmax: 6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Carbonic anhydrase 2 PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Carbonic Anhydrase 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, 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 5.10 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: X33
Carbonic anhydrase 2
Mol. type   Protein
Organism   Bos taurus
Olig. state   Monomer
Mon. MW   29.1 kDa
 
UniProt   P00921
Sequence   FASTA
 
PDB ID   1V9E