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

Loukachevitch LV, Egli M
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 63 (Pt 2): 84-8

PMID: 17277445 · PMCID: PMC2330121 · DOI:10.1107/S1744309106055461

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 A resolution, respectively.

MeSH Terms (4)

Crystallography, X-Ray Escherichia coli Ribonuclease H RNA, Double-Stranded

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