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

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, ?=82.8, ?=68.2, ?=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%.

SUBMITTER: Cho JW

PROVIDER: S-EPMC3792672 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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

Cho Jea-Won JW Han Byeong-Gu BG Park Sang Youn SY Kim Seung Jun SJ Kim Myoung-Dong MD Lee Byung Il BI

Acta crystallographica. Section F, Structural biology and crystallization communications 20130928 Pt 10

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 crysta ...[more]

PMID: 24100564

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