Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis.
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.
Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques, UMR 7036 CNRS-UHP, Groupe Biocristallographie, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre-lès-Nancy, France.
Hélène
H
Dubourg
Claire
C
Stines-Chaumeil
Claude
C
Didierjean
François
F
Talfournier
Sophie
S
Rahuel-Clermont
Guy
G
Branlant
André
A
Aubry
D000445:Aldehyde Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D050646:Methylmalonate-Semialdehyde Dehydrogenase (Acylating)
D000445:Aldehyde Oxidoreductases; D050646:Methylmalonate-Semialdehyde Dehydrogenase (Acylating)