Purification and crystallization of RNase HIII from Staphylococcus aureus.
Purification and crystallization of RNase HIII from Staphylococcus aureus.
复制标题
金黄色葡萄球菌 RNase HIII 的纯化和结晶。
DOI：
10.1107/s1744309110045616
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Asojo,OluwatoyinA
中科院分区：
文献类型：
--
作者：
Reiling,ScottA;Homma,Kohei;Asojo,OluwatoyinA
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.
