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

doi:10.1107/S1744309105009152

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

Graduate School of Natural Science and Technology

Research output: Contribution to journal › Article › peer-review

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 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	https://doi.org/10.1107/S1744309105009152
Publication status	Published - 2005

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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Umena, Y., Yorita, K., Matsuoka, T., Abe, M., Kita, A., Fukui, K., Tsukihara, T., & Morimoto, Y. (2005). Crystallization and preliminary X-ray diffraction study of l-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(4), 439-441. https://doi.org/10.1107/S1744309105009152

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 › peer-review

Umena, Y, Yorita, K, Matsuoka, T, Abe, M, Kita, A, Fukui, K, Tsukihara, T & Morimoto, Y 2005, 'Crystallization and preliminary X-ray diffraction study of l-lactate oxidase (LOX), R181M mutant, from Aerococcus viridans', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 61, no. 4, pp. 439-441. https://doi.org/10.1107/S1744309105009152

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.

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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",

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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

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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.

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

Abstract

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