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

Journal Article · · Acta Crystallographica. Section F

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.

Research Organization:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Organization:
USDOE
OSTI ID:
1007573
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: (2) ; 02, 2007 Vol. 63; ISSN 1744-3091
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
ENGLISH

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