June 1, 2004
Journal Article

Crystallization and preliminary crystallographic analysis of an Enterococcus faecalis repressor protein, CylR2, involved in regulating cytolysin production through quorum-sensing

Abstract

CylR2 is one of the two regulatory proteins associated with the quorum-sensing-dependent synthesis of cytolysin for the common pathogen Enterococcus faecalis. The protein was expressed with a C-terminal 6-histidine tag and purified to homogeneity with a cobalt affinity column followed by another size exclusion column. Both native and SeMet proteins were crystallized. A complete X-ray diffraction data set from the native crystal was collected to 2.3 Å resolution. The crystal was tetragonal, belonging to space group P41/43, with unit-cell dimensions a=b=66.2 Å, c=40.9 Å and a=b=g=90°. The asymmetric unit contained two molecules of CylR2.

Revised: June 18, 2004 | Published: June 1, 2004

Citation

Ni S., K. McAteer, D.E. Bussiere, and M.A. Kennedy. 2004. Crystallization and preliminary crystallographic analysis of an Enterococcus faecalis repressor protein, CylR2, involved in regulating cytolysin production through quorum-sensing. Acta Crystallographica. Section D, Biological Crystallography 60, no. Part 6:1145-1148. PNWD-SA-6213.