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 - Dec 1 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