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Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from candida tropicalis
Journal article   Open access   Peer reviewed

Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from candida tropicalis

Li-Chun Chen, Sheng-Cih Huang, Phimonphan Chuankhayan, Chung-Der Chen, Yen-Chieh Huang, Jeyaraman Jeyakanthan, Hsiao-Fang Pang, Lee-Chung Men, Yu-Ching Chen, Yu-Kuo Wang, …
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol.65(4), pp.419-421
2009

Abstract

Candida tropicalis Xylose reductase
Xylose reductase (XR), which requires NADPH as a co-substrate, catalyzes the reduction of d-xylose to xylitol, which is the first step in the metabolism of d - xylose. The detailed three-dimensional structure of XR will provide a better understanding of the biological significance of XR in the efficient production of xylitol from biomass. XR of molecular mass 36.6 kDa from Candida tropicalis was crystallized using the hanging-drop vapour-diffusion method. According to X-ray diffraction data from C. tropicalis XR crystals at 2.91 Å resolution, the unit cell belongs to space group P31 or P32. Preliminary analysis indicated the presence of four XR molecules in the asymmetric unit, with 68.0% solvent content. © 2009 International Union of Crystallography All rights reserved.
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https://doi.org/10.1107/S1744309109008719View
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