Standard proteins

Erica Valentini.

SASDAK6 – Glucose Isomerase

Xylose isomerase
MWI(0) 184.0 kDa
MWexpected 172 kDa
VPorod 293.1 nm3
log I(s) 1.65×102 1.65×101 1.65×100 1.65×10-1
Xylose isomerase small angle scattering data  s, nm-1
ln I(s)
Xylose isomerase Guinier plot ln 1.65×102 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
Xylose isomerase Kratky plot 1.104 0 3 sRg
p(r)
Xylose isomerase pair distance distribution function Rg: 3.3 nm 0 Dmax: 9.7 nm

Experimental data validation


Fits and models


log I(s)
 s, nm-1
Xylose isomerase DAMMIF model
log I(s)
 s, nm-1
Xylose isomerase PDB model
Synchrotron SAXS data from solutions of Glucose Isomerase in PBS, 50% Glycerol, 0.076 M NaCl, pH 7.4 were collected on the X33 camera on the storage ring DORIS III (Hamburg, Germany). Using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm , the range of momentum transfer 0.087 < s < 6.170 nm-1 was covered (s = 4π sin θ/λ, where 2θ is the scattering angle). Solute concentrations ranging between 1.2 and 12.8 mg/ml were measured . 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 and the different curves were scaled for protein concentration. 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.

Xylose isomerase
Mol. type   Protein
Organism   Streptomyces rubiginosus
Olig. state   Tetramer
Mon. MW   43.2 kDa
 
UniProt   P24300
Sequence   FASTA
 
PDB code   1OAD