title: Crystallization and preliminary diffraction studies of hydroxypyruvate reductase (D-glycerate dehydrogenase) from Hyphomicrobium methylovorum.
abstract: Two crystal forms of hydroxypyruvate reductase (D-glycerate dehydrogenase) from the methylotrophic bacterium Hyphomicrobium methylovorum have been grown from ammonium sulphate solutions. One crystal form is triclinic, with unit cell parameters a = 60.4 A, b = 60.5 A, c = 66.3 A, alpha = 102.3 degrees, beta = 113.7 degrees and gamma = 102.7 degrees, suggesting that a dimer (monomer M(r) 38,000) occupies the unit cell. This crystal form diffracts to beyond 2.4 A resolution and is suitable for crystallographic structure analysis.
authors.affiliation: Imperial College, London, U.K.
authors.forename: J D
authors.initials: JD
authors.lastname: Goldberg
authors.forename: P
authors.initials: P
authors.lastname: Brick
authors.forename: T
authors.initials: T
authors.lastname: Yoshida
authors.forename: T
authors.initials: T
authors.lastname: Mitsunaga
authors.forename: T
authors.initials: T
authors.lastname: Oshiro
authors.forename: M
authors.initials: M
authors.lastname: Shimao
authors.forename: Y
authors.initials: Y
authors.lastname: Izumi
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000648:ultrastructure; D001419:Bacteria / Q000201:enzymology; D003461:Crystallography; D050537:Hydroxypyruvate Reductase; D014961:X-Ray Diffraction
chemical_list: D000429:Alcohol Oxidoreductases; D050537:Hydroxypyruvate Reductase