Standard proteins

Erica Valentini.

SASDAK6 – Glucose Isomerase

Xylose isomerase
MWI(0) 184 kDa
MWexpected 172 kDa
VPorod 293 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

Data validation

Fits and models

log I(s)
 s, nm-1
Xylose isomerase DAMMIF model
log I(s)
 s, nm-1
Xylose isomerase PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Glucose Isomerase in PBS, 50% Glycerol, 0.076 M NaCl, pH 7.4 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (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 (I(s) vs s, where s = 4πsinθ/λ, and 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. 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.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Tags: X33
Xylose isomerase
Mol. type   Protein
Organism   Streptomyces rubiginosus
Olig. state   Tetramer
Mon. MW   43.2 kDa
 
UniProt   P24300
Sequence   FASTA
 
PDB ID   1OAD