Crystallization and preliminary X-ray analysis of Escherichia coli RNase G.
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.
Fang
Pengfei
P
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
Wang
Jing
J
Li
Xu
X
Guo
Min
M
Xing
Li
L
Cao
Xu
X
Zhu
Yi
Y
Gao
Yan
Y
Niu
Liwen
L
Teng
Maikun
M
D000595:Amino Acid Sequence; D003460:Crystallization; D003625:Data Collection; D019281:Dimerization; D004722:Endoribonucleases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013223:Statistics as Topic; D013440:Sulfides / Q000737:chemistry; D014961:X-Ray Diffraction
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D013440:Sulfides; D004722:Endoribonucleases; C081905:rng protein, E coli