title: Crystallization and preliminary crystallographic analysis of NADPH:FMN oxidoreductase from Vibrio harveyi.
abstract: Crystals of NADPH:FMN oxidoreductase from Vibrio harveyi have been obtained and characterized by X-ray diffraction. This enzyme plays a role in the generation of light in luminescent bacteria by providing reduced FMN to luciferase. Large, high quality crystals were grown using polyethylene glycol 6000 at pH 7.0. They crystallize in the monoclinic space group P2(1) with cell dimensions a = 51.2 A, b = 85.9 A, c = 58.1 A, beta = 109.3 degrees, and diffract to 1.8 A. We expect two molecules per asymmetric unit. High resolution data sets have been recorded and a search is under way for heavy-atom derivatives.
authors.affiliation: Department of Biochemistry and Biophysical Sciences, University of Houston, TX 77204-5934.
authors.forename: J
authors.initials: J
authors.lastname: Tanner
authors.forename: B
authors.initials: B
authors.lastname: Lei
authors.forename: M
authors.initials: M
authors.lastname: Liu
authors.forename: S C
authors.initials: SC
authors.lastname: Tu
authors.forename: K L
authors.initials: KL
authors.lastname: Krause
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D038181:FMN Reductase; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D011092:Polyethylene Glycols / Q000737:chemistry; D014733:Vibrio / Q000201:enzymology*
chemical_list: D011092:Polyethylene Glycols; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases