Purification, crystallization and X-ray crystallographic analysis of methylglyoxal reductase Gre2 from Candida albicans

Methylglyoxal reductase Gre2 converts methylglyoxal to lactaldehyde, using either NADH or NADPH as electron donor, to protect cells from the cytotoxic effects of methylglyoxal. Gre2 belongs to the short-chain dehydrogenase/reductase superfamily, which exhibits considerable variation in its substrate binding clefts to catalyze a broad range of substrates. In this study, to understand the structural features and molecular mechanism of Gre2, we overexpressed, purified, and crystallized the N-terminal His6-tagged Gre2 protein from Candida albicans and obtained X-ray diffraction data at a resolution of 2.8 Å. The C. albicans Gre2 crystal belongs to space group I23 with unit cell parameters a = b = c = 149.6 Å, α = β = γ = 90º. There is one molecule in the asymmetric unit.