Crystallization and preliminary X-ray diffraction analysis of the Bacillus subtilis replication termination protein in complex with the 37-base-pair TerI-binding site

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2006-11, Vol.62 (11), p.1104-1107
• Main Authors: Vivian, J. P., Porter, C., Wilce, J. A., Wilce, M. C. J.
• Format: Article
• Language: English
• Subjects: Bacillus subtilis; Bacillus subtilis - chemistry; Bacillus subtilis - genetics; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Base Pairing; Binding Sites; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; Crystallization Communications; CRYSTALS; DNA; DNA, Bacterial - chemistry; DNA, Bacterial - genetics; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - isolation & purification; Mutagenesis, Site-Directed; PROTEINS; Recombinant Proteins - chemistry; replication terminator proteins; RESOLUTION; SPACE GROUPS; SYNCHROTRON RADIATION; TerI; Terminator Regions, Genetic; X-RAY DIFFRACTION
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309106039108

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 Rsym of 12% was collected from a single flash‐cooled crystal using synchrotron radiation. The diffraction data are consistent with space group P622, with unit‐cell parameters a = b = 118.8, c = 142.6 Å.