Open AccessCrystallization and preliminary X‐ray crystallographic studies of DesR, a thermosensing response regulator in a two‐component signalling system from Streptococcus pneumoniae
Author(s) -
Park Ae Kyung,
Bong Seung Min,
Moon Jin Ho,
Chi Young Min
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109023082
Subject(s) - regulator , response regulator , streptococcus pneumoniae , crystallization , component (thermodynamics) , signalling , crystallography , materials science , microbiology and biotechnology , chemistry , biology , physics , bacterial protein , biochemistry , gene , thermodynamics , antibiotics , organic chemistry
The response regulator DesR, which activates the transcription of the des gene by binding to a regulatory region, is essential for controlling the fluidity of membrane phospholipids. DesR from Streptococcus pneumoniae was overexpressed in Escherichia coli . The protein was purified and crystallized for structural analysis. Diffraction data were collected to 1.7 Å resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 46.91, b = 71.38, c = 117.73 Å. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V M of 2.21 Å 3 Da −1 .