title: Crystallization and preliminary X-ray diffraction study of L-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans.
abstract: L-Lactate oxidase (LOX) from Aerococcus viridans is a member of the alpha-hydroxyacid oxidase flavoenzyme family. An X-ray crystallographic study of a LOX mutant in which Arg181 is replaced by Met was initiated in order to understand the functions of the conserved amino-acid residues around the FMN in the enzyme active site. LOX-R181M crystals belong to the tetragonal space group I422, with unit-cell parameters a = b = 192.632, c = 200.263 A, alpha = beta = gamma = 90 degrees. There are four monomers in the asymmetric unit. Diffraction data were collected under cryogenic conditions to 2.44 A resolution from LOX-R181M crystals at BL41XU, SPring-8.
authors.affiliation: Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan.
authors.forename: Yasufumi
authors.initials: Y
authors.lastname: Umena
authors.forename: Kazuko
authors.initials: K
authors.lastname: Yorita
authors.forename: Takeshi
authors.initials: T
authors.lastname: Matsuoka
authors.forename: Makoto
authors.initials: M
authors.lastname: Abe
authors.forename: Akiko
authors.initials: A
authors.lastname: Kita
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Fukui
authors.forename: Tomitake
authors.initials: T
authors.lastname: Tsukihara
authors.forename: Yukio
authors.initials: Y
authors.lastname: Morimoto
mesh_terms: D001665:Binding Sites; D017124:Conserved Sequence; D003460:Crystallization; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000235:genetics; D020125:Mutation, Missense; D034363:Viridans Streptococci / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D006899:Mixed Function Oxygenases; C021497:lactate 2-monooxygenase