Crystallization and preliminary crystallographic analysis of an Enterococcus faecalis repressor protein, CylR2, involved in regulating cytolysin production through quorum-sensing
CylR2 is one of two regulatory proteins associated with the quorum-sensing-dependent synthesis of cytolysin in the common pathogen Enterococcus faecalis. The protein was expressed with a C-terminal six-histidine tag and purified to homogeneity with a cobalt-affinity column followed by size-exclusion chromatography. Both native and SeMet proteins were produced and crystallized. Complete X-ray diffraction data sets were collected from a native crystal, which diffracted to 2.3 Å resolution, and a SeMet crystal, which diffracted to 2.1 Å. The crystals were tetragonal, belonging to space group P41 or P43, with unit-cell parameters a = b = 66.2, c = 40.9 Å, α = = = 90°. Based on the calculated Matthews coefficient of 2.6 Å3 Da−1 as well as analysis of anomalous difference Patterson maps, the asymmetric unit most likely contains two molecules of CylR2.
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