Protein expression, crystallization and preliminary X-ray crystallographic studies on HSCARG from Homo sapiens.
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.
Dai
Xueyu
X
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, P. R. China. xiaofengz@pku.edu.cn.
Gu
Xiaocheng
X
Luo
Ming
M
Zheng
Xiaofeng
X
D000595:Amino Acid Sequence; D003460:Crystallization; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D005656:Fungal Proteins; C520476:NMRAL1 protein, human; D014157:Transcription Factors; D010088:Oxidoreductases