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
C2 - 16511063
AN - SCOPUS:33744486908
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 -