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

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 Ê , and contain one tetramer per asymmetric unit. X-ray diffraction data were collected to 2.5 A Ê resolution using a synchrotron-radiation source. The crystal structure was solved by the molecular-replacement method.
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https://hal.univ-lorraine.fr/hal-01681502
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Hélène Dubourg, Claire Stines-Chaumeil, Claude Didierjean, Francois Talfournier, Sophie Rahuel-Clermont, et al.. Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis. Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2004, 60 (8), pp.1435 - 1437. ⟨10.1107/S0907444904012533⟩. ⟨hal-01681502⟩

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