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Crystallization and preliminary X-ray analysis of Escherichia coli RNase G.

Authors :
Fang, Pengfei
Wang, Jing
Li, Xu
Guo, Min
Xing, Li
Cao, Xu
Zhu, Yi
Gao, Yan
Niu, Liwen
Teng, Maikun
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Jun2009, Vol. 65 Issue 6, p586-588. 3p.
Publication Year :
2009

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 Å. X-ray diffraction data were collected to a resolution of 3.4 Å. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
65
Issue :
6
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
110812231
Full Text :
https://doi.org/10.1107/S1744309109015802