Open AccessCrystallization and preliminary X‐ray diffraction analysis of the DNA‐binding domain of the response regulator SaeR from Staphylococcus epidermidis
Author(s) -
Chen ShengChia,
Huang ChiHung,
Chen YuRen,
Yang Chia Shin,
Lin ChingTing,
Chen Yeh
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113012943
Subject(s) - staphylococcus epidermidis , effector , crystallization , dna binding domain , biophysics , dna , crystallography , biology , chemistry , microbiology and biotechnology , biochemistry , genetics , transcription factor , bacteria , staphylococcus aureus , organic chemistry , gene
SaeR is the response regulator of the SaeRS two‐component signal transduction system, which is involved in regulating bacterial autolysis and biofilm formation. SaeR comprises an N‐terminal receiver domain and a C‐terminal effector domain. The effector domain possesses DNA‐binding and transactivation functions. Here, the effector domain of SaeR from Staphylococcus epidermidis was purified and crystallized using the sitting‐drop vapour‐diffusion method. The crystals diffracted to a resolution of 2.15 Å and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 34.20, b = 53.78, c = 111.66 Å. Determining the structure will provide insights into the mechanisms underlying DNA binding.