Open AccessCrystallization and preliminary X‐ray diffraction analysis of the Bacillus subtilis replication termination protein in complex with the 37‐base‐pair TerI‐binding site
Author(s) -
Vivian J. P.,
Porter C.,
Wilce J. A.,
Wilce M. C. J.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106039108
Subject(s) - bacillus subtilis , crystallization , replication (statistics) , crystallography , base (topology) , binding site , diffraction , chemistry , biology , physics , mathematics , genetics , biochemistry , optics , virology , bacteria , mathematical analysis , organic chemistry
The replication terminator protein (RTP) of Bacillus subtilis binds to specific DNA sequences that halt the progression of the replisome in a polar manner. These terminator complexes flank a defined region of the chromosome into which they allow replication forks to enter but not exit. Forcing the fusion of replication forks in a specific zone is thought to allow the coordination of post‐replicative processes. The functional terminator complex comprises two homodimers each of 29 kDa bound to overlapping binding sites. A preparation of RTP and a 37‐base‐pair TerI sequence (comprising two binding sites for RTP) has been purified and crystallized. A data set to 3.9 Å resolution with 97.0% completeness and an R sym of 12% was collected from a single flash‐cooled crystal using synchrotron radiation. The diffraction data are consistent with space group P 622, with unit‐cell parameters a = b = 118.8, c = 142.6 Å.