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Overexpression, crystallization and preliminary X‐ray analysis of xylulose‐5‐phosphate/fructose‐6‐phosphate phosphoketolase from Bifidobacterium breve

Overexpression, crystallization and preliminary X‐ray analysis of... The xylulose‐5‐phosphate/fructose‐6‐phosphate phosphoketolase gene from Bifidobacterium breve was cloned and overexpressed in Escherichia coli. The enzyme was purified to homogeneity and crystallized by the sitting‐drop vapour‐diffusion method. Crystals were obtained at 293 K using 0.05 mM thiamine diphosphate, 0.25 mM MgCl2, 24%(w/v) PEG 6000 and 0.1 M Bicine pH 9.0. The crystals belonged to the tetragonal space group I422, with unit‐cell parameters a = b = 174.8, c = 163.8 Å, and diffracted to beyond 1.7 Å resolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Overexpression, crystallization and preliminary X‐ray analysis of xylulose‐5‐phosphate/fructose‐6‐phosphate phosphoketolase from Bifidobacterium breve

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References (30)

Publisher
Wiley
Copyright
International Union of Crystallography, 2010
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309110023845
pmid
20693675
Publisher site
See Article on Publisher Site

Abstract

The xylulose‐5‐phosphate/fructose‐6‐phosphate phosphoketolase gene from Bifidobacterium breve was cloned and overexpressed in Escherichia coli. The enzyme was purified to homogeneity and crystallized by the sitting‐drop vapour‐diffusion method. Crystals were obtained at 293 K using 0.05 mM thiamine diphosphate, 0.25 mM MgCl2, 24%(w/v) PEG 6000 and 0.1 M Bicine pH 9.0. The crystals belonged to the tetragonal space group I422, with unit‐cell parameters a = b = 174.8, c = 163.8 Å, and diffracted to beyond 1.7 Å resolution.

Journal

Acta Crystallographica Section FWiley

Published: Aug 1, 2010

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