Protein Expression, Crystallization and Preliminary X-Ray Crystallographic Studies on HSCARG from Homo Sapiens

Authors: Dai, Xueyu; Gu, Xiaocheng; Luo, Ming; Zheng, Xiaofeng

Source: Protein and Peptide Letters, Volume 13, Number 9, September 2006 , pp. 955-957(3)

Publisher: Bentham Science Publishers

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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 Å on Mar225 CCD Detector at SER-CAT 22BM synchrotron source. The crystals belong to F23 space group, with unit cell parameters a=b=c=223.30Å, α=β=γ=90°. There are two molecules per asymmetry unit.

Keywords: HSCARG; Homo sapiens; protein crystallography

Document Type: Research Article


Affiliations: Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing,100871, China.

Publication date: September 1, 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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