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 - 2005
Externally publishedYes

Fingerprint

lactate 2-monooxygenase
Aerococcus
lactates
oxidase
Crystallization
X-Ray Diffraction
crystallization
X ray diffraction
diffraction
x rays
Flavin Mononucleotide
Crystals
Cryogenics
Catalytic Domain
Oxidoreductases
Diffraction
Monomers
X-Rays
crystals
cryogenics

ASJC Scopus subject areas

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

Cite this

Crystallization and preliminary X-ray diffraction study of l-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans. / Umena, Yasufumi; Yorita, Kazuko; Matsuoka, Takeshi; Abe, Makoto; Kita, Akiko; Fukui, Kiyoshi; Tsukihara, Tomitake; Morimoto, Yukio.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 4, 2005, p. 439-441.

Research output: Contribution to journalArticle

Umena, Yasufumi ; Yorita, Kazuko ; Matsuoka, Takeshi ; Abe, Makoto ; Kita, Akiko ; Fukui, Kiyoshi ; Tsukihara, Tomitake ; Morimoto, Yukio. / Crystallization and preliminary X-ray diffraction study of l-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2005 ; Vol. 61, No. 4. pp. 439-441.
@article{a008a516ce3548179534316a67e980f4,
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 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 {\AA}, α = β = γ = 90°. There are four monomers in the asymmetric unit. Diffraction data were collected under cryogenic conditions to 2.44 {\AA} resolution from LOX-R181M crystals at BL41XU, SPring-8.",
author = "Yasufumi Umena and Kazuko Yorita and Takeshi Matsuoka and Makoto Abe and Akiko Kita and Kiyoshi Fukui and Tomitake Tsukihara and Yukio Morimoto",
year = "2005",
doi = "10.1107/S1744309105009152",
language = "English",
volume = "61",
pages = "439--441",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction study of l-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans

AU - Umena, Yasufumi

AU - Yorita, Kazuko

AU - Matsuoka, Takeshi

AU - Abe, Makoto

AU - Kita, Akiko

AU - Fukui, Kiyoshi

AU - Tsukihara, Tomitake

AU - Morimoto, Yukio

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=33744486908&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33744486908&partnerID=8YFLogxK

U2 - 10.1107/S1744309105009152

DO - 10.1107/S1744309105009152

M3 - Article

VL - 61

SP - 439

EP - 441

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 4

ER -