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Purification, crystallization and preliminary crystallographic analysis of a ribosome‐recycling factor from Thermoanaerobacter tengcongensis ( Tte RRF)
Author(s) -
Shang Guijun,
Feng Duo,
Lu Fang,
Zhang Hongjie,
Cang Huaixing,
Gao Wei,
Bi Ruchang
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1400507x
Subject(s) - crystallization , crystallography , elongation factor , chemistry , thermophile , ribosome , citric acid , crystal structure , biology , biochemistry , rna , organic chemistry , enzyme , gene
Ribosome‐recycling factor (RRF) plays an essential role in the fourth step of protein synthesis in prokaryotes. RRF combined with elongation factor G (EF‐G) disassembles the post‐termination ribosome complex and recycles the protein synthesis machine for the next round of translation. A reductive‐methylation‐modified RRF from Thermoanaerobacter tengcongensis ( TteRRF ) has been crystallized using the vapour‐diffusion method. The crystal grew in a condition consisting of 0.1 M citric acid pH 3.5, 3.0 M NaCl and 50 mg ml −1 methylated protein solution at 289 K. A complete data set was collected from a crystal to 2.80 Å resolution using synchrotron radiation at 100 K. The crystal belonged to space group P 6 1 22/ P 6 5 22 with unit‐cell parameters a = b = 103.26, c = 89.17 Å. The asymmetric unit was estimated to contain one molecule of Tte RRF.