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Purification and crystallization of RNase HIII from Staphylococcus aureus

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As part of collaborative efforts to characterize virulence factors from Staphylococcus aureus, methods for the large‐scale recombinant production of RNase HIII from S. aureus subspecies MRSA252 (Sa‐RNase HIII) have been developed. RNase HIII‐type ribonucleases are poorly characterized members of the RNase H group of endonucleases which hydrolyze RNA from RNA/DNA hybrids and are thought to be involved in DNA replication and repair. They are characterized by N‐terminal extensions of unknown function that do not share sequence homology with the N‐terminal extensions of bacterial RNases HI and RNases HII. Sa‐RNase HIII was crystallized in the orthorhombic space group P212121, with unit‐cell parameters a = 48.9, b = 74.2, c = 127.5 Å, and diffracted to 2.6 Å resolution.
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Keywords: MRSA; RNase HIII; RNases; Staphylococcus aureus

Document Type: Research Article

Affiliations: Department of Pathology and Microbiology, College of Medicine, Nebraska Medical Center, Omaha, NE 68198-6495, USA

Publication date: January 1, 2011

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