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

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

6 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
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309105009152

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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 et al.

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

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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",

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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

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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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