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- W2019933486 abstract "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." @default.
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- W2019933486 date "2006-10-20" @default.
- W2019933486 modified "2023-09-27" @default.
- W2019933486 title "Crystallization and preliminary X-ray diffraction analysis of the<i>Bacillus subtilis</i>replication termination protein in complex with the 37-base-pair TerI-binding site" @default.
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- W2019933486 doi "https://doi.org/10.1107/s1744309106039108" @default.
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