The replication terminator protein (RTP)-DNA complex of Bacillus subtilis is responsible for the arrest of DNA replication at terminator sites in the B. subtilis chromosome. The crystallization and preliminary diffraction data analysis for the complex of an 15N-labelled mutant form of RTP and a symmetrical form of its DNA-binding site is reported. NMR spectroscopy was used to assess the stoichiometry of complex formation, with the sample containing the most homogenous solution of complex giving rise to diffracting crystals. Synchrotron-radiation data to 2.5 Å were collected from a crystal of space group P3221, unit-cell parameters a = b = 44.780, c = 395.582 Å, containing an RTP dimer within the asymmetric unit.
|Number of pages||4|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - 21 Mar 2001|