Crystallization and preliminary X-ray diffraction study of l-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans

Yasufumi Umena, Kazuko Yorita, Takeshi Matsuoka, Makoto Abe, Akiko Kita, Kiyoshi Fukui, Tomitake Tsukihara, Yukio Morimoto

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

l-Lactate oxidase (LOX) from Aerococcus viridans is a member of the α-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 Å, α = β = γ = 90°. There are four monomers in the asymmetric unit. Diffraction data were collected under cryogenic conditions to 2.44 Å resolution from LOX-R181M crystals at BL41XU, SPring-8.

Original languageEnglish
Pages (from-to)439-441
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number4
DOIs
Publication statusPublished - Dec 1 2005

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray diffraction study of l-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans'. Together they form a unique fingerprint.

  • Cite this