Literature DB >> 17277445

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

Lioudmila V Loukachevitch1, Martin Egli.   

Abstract

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.

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Year:  2007        PMID： 17277445      PMCID： PMC2330121          DOI： 10.1107/S1744309106055461

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  39 in total

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Review 4.  Targeting the Virus Capsid as a Tool to Fight RNA Viruses.

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