Preparation, crystallization and preliminary X-ray analysis of protein YtlP from Bacillus subtilis

被引：1

作者：

Liu, Cong

Li, Dan

Hederstedt, Lars

Li, Lanfen

Liang, Yu-He ^{[1
]}

Su, Xiao-Dong

机构：

[1] Peking Univ, Natl Lab Prot Engn & Plant Genet Engn, Beijing 100871, Peoples R China

[2] Peking Univ, Dept Biochem & Mol Biol, Coll Life Sci, Beijing 100871, Peoples R China

[3] Lund Univ, Dept Cell & Organism Biol, SE-22362 Lund, Sweden

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷

关键词：

D O I：

10.1107/S174430910603199X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Bacillus subtilis YtlP is a protein that is predicted to belong to the bacterial and archael 2'-5' RNA-ligase family. It contains 183 residues and two copies of the HXTX sequence motif conserved among proteins belonging to this family. In order to determine the structure of YtlP and to compare it with the paralogue YjcG and identified 2'-5' RNA ligases, the gene ytlP was amplified from B. subtilis genomic DNA and cloned into expression vector pET-21a. The soluble protein was produced in Escherichia coli, purified to homogeneity and crystals suitable for X-ray analysis were obtained. The crystal diffracted to 2.0 angstrom and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.16, b = 48.54, c = 105.75 angstrom.

引用

页码：967 / 969

页数：3

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