Open AccessCrystallization and preliminary X‐ray analysis of Escherichia coli RNase G
Author(s) -
Fang Pengfei,
Wang Jing,
Li Xu,
Guo Min,
Xing Li,
Cao Xu,
Zhu Yi,
Gao Yan,
Niu Liwen,
Teng Maikun
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109015802
Subject(s) - escherichia coli , rnase p , crystallization , rnase h , recombinant dna , x ray crystallography , microbiology and biotechnology , biology , chemistry , biochemistry , crystallography , diffraction , rna , gene , physics , organic chemistry , optics
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 F 432, with unit‐cell parameters a = b = c = 219.84 Å. X‐ray diffraction data were collected to a resolution of 3.4 Å.