Open AccessPreparation, crystallization and preliminary X‐ray analysis of YjcG protein from Bacillus subtilis
Author(s) -
Li Dan,
Chan Chiomui,
Liang YuHe,
Zheng Xiaofeng,
Li Lanfen,
Su XiaoDong
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105011012
Subject(s) - bacillus subtilis , escherichia coli , biology , gene , homology (biology) , genomic dna , dna , microbiology and biotechnology , crystallization , rna , sequence analysis , biochemistry , chemistry , genetics , bacteria , organic chemistry
Bacillus subtilis YjcG is a functionally uncharacterized protein with 171 residues that has no structural homologue in the Protein Data Bank. However, it shows sequence homology to bacterial and archaeal 2′–5′ RNA ligases. In order to identify its exact function via structural studies, the yjcG gene was amplified from B. subtilis genomic DNA and cloned into the expression vector pET21‐DEST. The protein was expressed in a soluble form in Escherichia coli and was purified to homogeneity. Crystals suitable for X‐ray analysis were obtained that diffracted to 2.3 Å and belonged to space group C 2, with unit‐cell parameters a = 99.66, b = 73.93, c = 61.77 Å, β = 113.56°.