BioDesign 2023; 11(3): 45-49
Published online September 30, 2023
© Korean Society for Structural Biology
Jie Zhang1,2, Xue Bai1,2, Shanru He1,2 and Yongbin Xu1,2,*
1Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China
2Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China
Correspondence to: *email@example.com
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 Å3 Da–1 and 47.00%, respectively, assuming the asymmetric unit contained four recombinant protein molecules.