Open AccessExpression, purification, crystallization and preliminary X‐ray analysis of the receiver domain of Staphylococcus aureus LytR protein
Author(s) -
Shala Agnesa,
Patel Kevin H.,
GolemiKotra Dasantila,
Audette Gerald F.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113030972
Subject(s) - lysis , crystallization , effector , virulence , staphylococcus aureus , drop (telecommunication) , crystallography , bacteria , transcription (linguistics) , chemistry , microbiology and biotechnology , materials science , biology , biochemistry , gene , genetics , telecommunications , organic chemistry , computer science , linguistics , philosophy
The response‐regulatory protein LytR belongs to a family of transcription factors involved in the regulation of important virulence factors in pathogenic bacteria. The protein consists of a receiver domain and an effector domain, which play an important role in controlled cell death and lysis. The LytR receiver domain (LytR N ) has been overexpressed, purified and crystallized using the sitting‐drop and hanging‐drop vapour‐diffusion methods. The crystals grew as needles, with unit‐cell parameters a = b = 84.82, c = 157.3 Å, α = β = 90, γ = 120°. LytR N crystallized in space group P 6 1 22 and the crystals diffracted to a maximum resolution of 2.34 Å. Based on the Matthews coefficient ( V M = 5.44 Å 3 Da −1 ), one molecule is estimated to be present in the asymmetric unit.