Unknown

Dataset Information

0

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


ABSTRACT: 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, ? = ? = 90, ? = 120°. LytR(N) crystallized in space group P6122 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.

SUBMITTER: Shala A 

PROVIDER: S-EPMC3855734 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Shala Agnesa A   Patel Kevin H KH   Golemi-Kotra Dasantila D   Audette Gerald F GF  

Acta crystallographica. Section F, Structural biology and crystallization communications 20131129 Pt 12


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 parameter  ...[more]

Similar Datasets

| S-EPMC3943096 | biostudies-literature
| S-EPMC3080155 | biostudies-literature
| S-EPMC3936436 | biostudies-literature
| S-EPMC2805527 | biostudies-literature
| S-EPMC4461344 | biostudies-literature
| S-EPMC2664771 | biostudies-literature
| S-EPMC3107138 | biostudies-literature
| S-EPMC3606580 | biostudies-literature
| S-EPMC4014338 | biostudies-literature
| S-EPMC3079971 | biostudies-literature