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 language | English |
|---|---|
| Pages (from-to) | 439-441 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 61 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2005 |
| Externally published | Yes |
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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 journal › Article
}
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 -