title: Crystallization and preliminary X-ray crystallographic studies of DesR, a thermosensing response regulator in a two-component signalling system from Streptococcus pneumoniae.
abstract: 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 A resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 46.91, b = 71.38, c = 117.73 A. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V(M) of 2.21 A(3) Da(-1).
authors: Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea.
authors: Ae Kyung
authors: AK
authors: Park
authors: Seung Min
authors: SM
authors: Bong
authors: Jin Ho
authors: JH
authors: Moon
authors: Young Min
authors: YM
authors: Chi
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015398:Signal Transduction; D013296:Streptococcus pneumoniae / Q000737:chemistry*; D013696:Temperature
chemical_list: D001426:Bacterial Proteins