Expression, purification, crystallization and preliminary X‐ray analysis of the receiver domain of Staphylococcus aureus LytR protein. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Shala, Agnesa; Patel, Kevin H.; Golemi‐Kotra, Dasantila; Audette, Gerald F.
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1418
• Page End: 1421
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113030972
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>a</italic> = <italic>b</italic> = 84.82, <italic>c</italic> = 157.3 Å, α = β = 90, γ = 120°. LytR^N crystallized in space group <italic>P</italic>6₁22 and the crystals diffracted to a maximum resolution of 2.34 Å. Based on the Matthews coefficient (<italic>V</italic>_M = 5.44 ų Da⁻¹), one molecule is estimated to be present in the asymmetric unit.</p> </abstract>