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

Journal Article · Tue Jun 01 00:00:00 EDT 2004 · Acta Crystallographica. Section D, Biological Crystallography

DOI:https://doi.org/10.1107/S0907444904008078· OSTI ID:15007827

Ni, Shuisong; McAteer, Kathleen; Bussiere, Dirksen E; Kennedy, Michael A

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 resolution. The crystal was tetragonal, belonging to space group P41/43, with unit-cell dimensions a=b=66.2 , c=40.9 and a=b=g=90. The asymmetric unit contained two molecules of CylR2.

• Research Organization: Pacific Northwest National Lab., Richland, WA (US)
• Sponsoring Organization: US Department of Energy (US)
• DOE Contract Number: AC06-76RL01830
• OSTI ID: 15007827
• Report Number(s): PNWD-SA-6213; TRN: US200421%%223
• Journal Information: Acta Crystallographica. Section D, Biological Crystallography, Vol. 60, Issue Part 6; Other Information: PBD: 1 Jun 2004
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
AFFINITY
COBALT
CRYSTALLIZATION
DIMENSIONS
PATHOGENS
PRODUCTION
PROTEINS
RESOLUTION
SPACE GROUPS
SYNTHESIS
X-RAY DIFFRACTION
ENTEROCOCCUS FAECALIS
CY1R2
TRANSCRIPTIONAL FACTOR