Expression, purification, crystallization and preliminary X-ray analysis of the receiver domain of Staphylococcus aureus LytR protein

被引:3
|
作者
Shala, Agnesa [1 ]
Patel, Kevin H. [1 ]
Golemi-Kotra, Dasantila [1 ,2 ]
Audette, Gerald F. [1 ,2 ]
机构
[1] York Univ, Dept Chem, Toronto, ON M3J 1P3, Canada
[2] York Univ, Dept Biol, Toronto, ON M3J 1P3, Canada
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金
加拿大自然科学与工程研究理事会; 加拿大健康研究院;
关键词
MUREIN HYDROLASE ACTIVITY; CRYSTAL-STRUCTURE; REGULATORS; BACTERIA; OPERON;
D O I
10.1107/S1744309113030972
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom, alpha = beta = 90, gamma = 120 degrees. LytR(N) crystallized in space group P6(1)22 and the crystals diffracted to a maximum resolution of 2.34 angstrom. Based on the Matthews coefficient (V-M = 5.44 angstrom(3) Da(-1)), one molecule is estimated to be present in the asymmetric unit.
引用
收藏
页码:1418 / 1421
页数:4
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