Purification, crystallization and preliminary crystallographic analysis of a ribosome-recycling factor from Thermoanaerobacter tengcongensis (TteRRF)

被引：1

作者：

Shang, Guijun ^{[1
]}

Feng, Duo ^{[1
]}

Lu, Fang ^{[1
]}

Zhang, Hongjie ^{[2
]}

Cang, Huaixing ^{[1
]}

Gao, Wei ^{[1
,3
]}

Bi, Ruchang ^{[2
]}

机构：

[1] Beijing Forestry Univ, Coll Sci, Beijing 100083, Peoples R China

[2] Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China

[3] Beijing Forestry Univ, Natl Engn Lab Tree Breeding, Beijing 100083, Peoples R China

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

基金：

中国国家自然科学基金;

关键词：

ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; TERMINATION COMPLEX; RELEASE; CODON; RRF;

D O I：

10.1107/S2053230X1400507X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom resolution using synchrotron radiation at 100 K. The crystal belonged to space group P6(1)22/P6(5)22 with unit-cell parameters a = b = 103.26, c = 89.17 angstrom. The asymmetric unit was estimated to contain one molecule of TteRRF.

引用

页码：588 / 591

页数：4

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