Open AccessOverexpression, crystallization and preliminary X‐ray crystallographic analysis of a putative xylose isomerase from Bacteroides thetaiotaomicron
Author(s) -
Cho JeaWon,
Han ByeongGu,
Park Sang Youn,
Kim Seung Jun,
Kim MyoungDong,
Lee Byung Il
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113023877
Subject(s) - xylose isomerase , bacteroides thetaiotaomicron , crystallization , polyethylene glycol , isomerase , xylose , crystallography , escherichia coli , chemistry , crystal (programming language) , crystal structure , resolution (logic) , protein crystallization , bacteroides , biochemistry , biology , bacteria , organic chemistry , enzyme , artificial intelligence , fermentation , gene , computer science , programming language , genetics
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 P 1, 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 ( V M ) of 2.38 Å 3 Da −1 and a solvent content of 48.3%.