Crystallization and preliminary crystallographic analysis of the central domain of Drosophila Dribble, a protein that is essential for ribosome biogenesis

被引:1
作者
Cheng, Tat-Cheung [1 ,2 ]
Chen, Yu Wai [3 ]
Wong, Kam-Bo [1 ,2 ,4 ]
Chan, H. Y. Edwin [1 ,2 ,4 ]
机构
[1] Chinese Univ Hong Kong, Dept Biochem, Hong Kong, Hong Kong, Peoples R China
[2] Chinese Univ Hong Kong, Mol Biotechnol Programme, Hong Kong, Hong Kong, Peoples R China
[3] Kings Coll London, Randall Div Cell & Mol Biophys, London SE1 1UL, England
[4] Chinese Univ Hong Kong, Cell & Mol Biol Programme, Hong Kong, Hong Kong, Peoples R China
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词
KRR1P; RNA; HOMOLOG; REVEALS;
D O I
10.1107/S1744309110011206
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Dribble (DBE) is a Drosophila protein that is essential for ribosome biogenesis. Bioinformatics analysis revealed a folded central domain of DBE which is flanked by structural disorder in the N- and C-terminal regions. The protein fragment spanning amino-acid residues 16-197 (DBE16-197) was produced for structural determination. In this report, the crystallization and preliminary X-ray diffraction data analysis of the DBE16-197 protein domain are described. Crystals of DBE16-197 were grown by the sitting-drop vapour-diffusion method at 289 K using ammonium phosphate as a precipitant. The crystals belonged to space group P2(1)2(1)2(1). Data were collected that extended to beyond 2 angstrom resolution.
引用
收藏
页码:546 / 548
页数:3
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