Candida auris is a new fungus that poses a serious global health threat due to its resistance to multiple antifungal medications, making treatment challenging. Aldo-keto reductase (AKR) represents a versatile superfamily of enzymes that play pivotal roles in the phase I metabolism of various metabolic and detoxification processes. In this study, AKR from C. auris (CaAldO) was successfully expressed and purified using Ni-NTA affinity, Q anion exchange, and gel-filtration chromatography. The protein crystal was obtained and diffracted to a resolution of 1.95 Å. The crystal belonged to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters of a = 71.65, b = 91.15, and c = 227.66 Å. The Matthews coefficient and solvent content were estimated to be 2.32 ų Da^–1 and 47.00%, respectively, assuming the asymmetric unit contained four recombinant protein molecules.