| Literature DB >> 19478437 |
Pengfei Fang1, Jing Wang, Xu Li, Min Guo, Li Xing, Xu Cao, Yi Zhu, Yan Gao, Liwen Niu, Maikun Teng.
Abstract
The homologous RNases RNase E and RNase G are widely distributed in bacteria and function in many important physiological processes, including mRNA degradation, rRNA maturation and so on. In this study, the crystallization and preliminary X-ray analysis of RNase G from Escherichia coli is described. Purified recombinant E. coli RNase G, which has 497 amino acids, was crystallized in the cubic space group F432, with unit-cell parameters a = b = c = 219.84 A. X-ray diffraction data were collected to a resolution of 3.4 A.Entities:
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Year: 2009 PMID: 19478437 PMCID: PMC2688416 DOI: 10.1107/S1744309109015802
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091