Open AccessPreparation, crystallization and preliminary X‐ray analysis of protein YtlP from Bacillus subtilis
Author(s) -
Liu Cong,
Li Dan,
Li Lanfen,
Hederstedt Lars,
Su XiaoDong,
Liang YuHe
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910603199x
Subject(s) - bacillus subtilis , escherichia coli , gene , biology , genomic dna , microbiology and biotechnology , rna , dna , chemistry , genetics , bacteria
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 H X T X 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 Å and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 34.16, b = 48.54, c = 105.75 Å.