Crystallization and preliminary X-ray analysis of Escherichia coli RNase HI-dsRNA complexes

被引：4
|
作者：
Loukachevitch, Lioudmila V. [1 ]
Egli, Martin [1 ]
机构：
[1] Vanderbilt Univ, Dept Biochem, Sch Med, Nashville, TN 37232 USA
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词：
D O I：
10.1107/S1744309106055461
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
RNase H binds RNA-DNA hybrid and double-stranded RNA (dsRNA) duplexes with similar affinity, but only cleaves the RNA in the former. To potentially gain insight into the conformational origins of substrate recognition by the enzyme from Escherichia coli, cocrystallization experiments were carried out with RNase HI-dsRNA (enzyme-inhibitor) complexes. Crystals were obtained of two complexes containing 9-mer and 10-mer RNA duplexes that diffracted X-rays to 3.5 and 4 angstrom resolution, respectively.
引用
收藏
页码：84 / 88
页数：5
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