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Updated: Jun 29, 2026
Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
Protein expression, crystallization and preliminary X-ray crystallographic studies on HSCARG from Homo sapiens
Xueyu Dai1, Xiaocheng Gu, Ming Luo
1National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, P. R. China. xiaofengz@pku.edu.cn.
Abstract:
Human HSCARG has been annotated as a possible cancer related protein. Amino acid homology, although at a low percentage, suggested that HSCARG contains NmrA domain and might be a member of short chain dehydrogenase reductase superfamily. In order to investigate its structure and function, HSCARG gene has been successfully expressed and purified in E. coli. HSCARG was crystallized and diffracted to a resolution of 2.4 A on Mar225 CCD Detector at SER-CAT 22BM synchrotron source. The crystals belong to F23 space group, with unit cell parameters a=b=c=223.30A, alpha=beta=gamma=90 degrees . There are two molecules per asymmetry unit.
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