Overexpression, crystallization and preliminary X-ray crystallographic analysis of a putative xylose isomerase from Bacteroides thetaiotaomicron

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1127-30. doi: 10.1107/S1744309113023877. Epub 2013 Sep 28.

Abstract

Bacteroides thetaiotaomicron BT0793, a putative xylose isomerase, was overexpressed in Escherichia coli, purified and crystallized using polyethylene glycol monomethyl ether 550 as the precipitant. X-ray diffraction data were collected to 2.10 Å resolution at 100 K using synchrotron X-rays. The crystal was found to belong to space group P1, with unit-cell parameters a=96.3, b=101.7, c=108.3 Å, α=82.8, β=68.2, γ=83.0°. The asymmetric unit contained eight subunits of xylose isomerase with a crystal volume per protein weight (VM) of 2.38 Å3 Da(-1) and a solvent content of 48.3%.

Keywords: BT0793; Bacteroides thetaiotaomicron; glucose isomerase; xylose isomerase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldose-Ketose Isomerases / chemistry*
  • Bacteroides / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Ketoses / chemistry
  • Ketoses / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Ketoses
  • Recombinant Proteins
  • Aldose-Ketose Isomerases
  • xylose isomerase