Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 66, Issue -, Pages 941-943Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110023845
Keywords
xylulose-5-phosphate; fructose-6-phosphate phosphoketolase; Bifidobacterium breve; bifid shunt; heterofermentative lactic acid bacteria
Funding
- Program for the Promotion of Basic Research Activities for Innovative Bioscience (PROBRAIN) in Japan
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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 A, and diffracted to beyond 1.7 A resolution.
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