Open AccessExpression, purification, crystallization and preliminary X‐ray diffraction data of methylmalonate‐semialdehyde dehydrogenase from Bacillus subtilis
Author(s) -
Dubourg Hélène,
StinesChaumeil Claire,
Didierjean Claude,
Talfournier François,
RahuelClermont Sophie,
Branlant Guy,
Aubry André
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904012533
Subject(s) - bacillus subtilis , tetramer , ammonium sulfate , crystallography , escherichia coli , x ray crystallography , diffraction , crystallization , chemistry , dehydrogenase , synchrotron radiation , resolution (logic) , optics , biology , bacteria , enzyme , biochemistry , physics , gene , chromatography , genetics , organic chemistry , artificial intelligence , computer science
Methylmalonate‐semialdehyde dehydrogenase from Bacillus subtilis was cloned and overexpressed in Escherichia coli . Suitable crystals for X‐ray diffraction experiments were obtained by the hanging‐drop vapour‐diffusion method using ammonium sulfate as precipitant. The crystals belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 195.2, b = 192.5, c = 83.5 Å, and contain one tetramer per asymmetric unit. X‐ray diffraction data were collected to 2.5 Å resolution using a synchrotron‐radiation source. The crystal structure was solved by the molecular‐replacement method.
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