title: Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynebacterium glutamicum.
abstract: A monomeric isocitrate dehydrogenase has been crystallized for the first time. This enzyme catalyzes the conversion of isocitrate to oxalosuccinate and subsequently to alpha-ketoglutarate and CO(2); the coenzyme NADP(+) is reduced to NADPH during the reaction. Polyethylene glycol 2000 monomethyl ether was used to crystallize the enzyme in space group C2 with unit-cell parameters a = 137.1, b = 54.6, c = 126.4 A, beta = 108.2 degrees. The very small crystal (0. 05 x 0.20 x 0.05 mm) diffracted to 3.5 A d spacing using synchrotron radiation.
authors.affiliation: Department of Biochemistry, University of Saskatchewan, 107 Wiggins Road, Saskatoon SK, S7K 5E5, Canada.
authors.forename: G F
authors.initials: GF
authors.lastname: Audette
authors.forename: J W
authors.initials: JW
authors.lastname: Quail
authors.forename: K
authors.initials: K
authors.lastname: Hayakawa
authors.forename: C
authors.initials: C
authors.lastname: Bai
authors.forename: R
authors.initials: R
authors.lastname: Chen
authors.forename: L T
authors.initials: LT
authors.lastname: Delbaere
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003352:Corynebacterium / Q000201:enzymology*; D003460:Crystallization; D019281:Dimerization; D007521:Isocitrate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D007521:Isocitrate Dehydrogenase; C039355:isocitrate dehydrogenase (NADP+)