Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 69, Issue -, Pages 934-936Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309113019672
Keywords
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Funding
- Key Projects in the National Science and Technology Pillar Program
- National Biological Medicine International Innovation Garden Special [12ZCZDSY10600]
- National Natural Science Foundation of China [81102374]
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Alanine dehydrogenase (L-AlaDH) from Bacillus megaterium WSH-002 catalyses the NAD(+)-dependent interconversion of L-alanine and pyruvate. The enzyme was expressed in Escherichia coli BL21 (DE3) cells and purified with a His(6) tag by Ni2+-chelating affinity chromatography for X-ray crystallographic analysis. Crystals were grown in a solution consisting of 0.1 M HEPES pH 8.0, 12%(w/v) polyethylene glycol 8000, 8%(v/v) ethylene glycol at a concentration of 15 mg ml(-1) purified protein. The crystal diffracted to 2.35 angstrom resolution and belonged to the trigonal space group R32, with unit-cell parameters a = b = 125.918, c = 144.698 angstrom.
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