title: Purification and crystallization of RNase HIII from Staphylococcus aureus.
abstract: 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 P2(1)2(1)2(1), with unit-cell parameters a=48.9, b=74.2, c=127.5 Å, and diffracted to 2.6 Å resolution.
authors.affiliation: Department of Pathology and Microbiology, College of Medicine, Nebraska Medical Center, Omaha, NE 68198-6495, USA.
authors.forename: Scott A
authors.initials: SA
authors.lastname: Reiling
authors.forename: Kohei
authors.initials: K
authors.lastname: Homma
authors.forename: Oluwatoyin A
authors.initials: OA
authors.lastname: Asojo
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D055624:Methicillin-Resistant Staphylococcus aureus / Q000201:enzymology*; D008969:Molecular Sequence Data; D012260:Ribonucleases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*
chemical_list: D001426:Bacterial Proteins; D012260:Ribonucleases; C117079:ribonuclease HIII