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PubMed · 15272169

Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis.

Hélène Dubourg·Claire Stines-Chaumeil·Claude Didierjean·François Talfournier·Sophie Rahuel-Clermont·Guy Branlant·André Aubry
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Abstract

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 P2(1)2(1)2(1), with unit-cell parameters a = 195.2, b = 192.5, c = 83.5 A, and contain one tetramer per asymmetric unit. X-ray diffraction data were collected to 2.5 A resolution using a synchrotron-radiation source. The crystal structure was solved by the molecular-replacement method.

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Aldehyde OxidoreductasesBacillus subtilisCrystallizationCrystallography, X-RayGene ExpressionMethylmalonate-Semialdehyde Dehydrogenase (Acylating)Journal Article

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Hélène Dubourg, Claire Stines-Chaumeil, Claude Didierjean, François Talfournier, Sophie Rahuel-Clermont, Guy Branlant, André Aubry. 2004-07-21. Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis.. https://doi.org/10.1107/s0907444904012533

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