Open AccessPurification, crystallization and preliminary X‐ray analysis of the effector domain of AlsR, an LysR‐type transcriptional regulator from Bacillus subtilis
Author(s) -
Frädrich Claudia,
Krausze Joern,
Quade Nick,
Heinz Dirk,
Jahn Dieter,
Härtig Elisabeth
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113010725
Subject(s) - bacillus subtilis , operon , effector , transcriptional regulation , regulator , escherichia coli , lac operon , transcription (linguistics) , biology , bacteria , chemistry , transcription factor , biochemistry , gene , genetics , linguistics , philosophy
AlsR from Bacillus subtilis , a member of the LysR‐type transcriptional regulator (LTTR) family, regulates the transcription of the alsSD operon encoding enzymes involved in acetoin biosynthesis. LTTRs represent the largest known family of transcriptional regulators in bacteria. In this study, AlsR 82–302 S100A, representing the effector domain, was produced in Escherichia coli , purified and crystallized using the sitting‐drop vapour‐diffusion method in the presence of 2.1 M DL‐malic acid pH 7.0 at 293 K. The crystals belonged to space group C 2, with unit‐cell parameters a = 142.91, b = 74.96, c = 94.39 Å, β = 110.543°. X‐ray data extending to a resolution of 2.6 Å were collected.