Abstract
Mouse vas deferens protein/aldo-keto reductase 1B7 (AKR1B7) is involved in the detoxification of isocaproaldehyde, a steroidogenesis byproduct, and of 4-hydroxynonenal formed by lipid peroxidation. The rat orthologue of AKR1B7 has recently been named AKR1B14 in the AKR superfamily. Recombinant AKR1B14 was expressed in a bacterial system and purified to homogeneity. The purified protein was crystallized from polyethylene glycol solutions using the hanging-drop vapour-diffusion method and an X-ray diffraction data set was collected to 1.86 A resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.66, b = 69.14, c = 72.27 A, beta = 96.4 degrees. This is the first crystallization report of a rodent AKR1B7 orthologue.