Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy

Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):421-4. doi: 10.1107/s0907444900019508.

Abstract

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 (15)N-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 homogeneous solution of complex giving rise to diffracting crystals. Synchrotron-radiation data to 2.5 A were collected from a crystal of space group P3(2)21, unit-cell parameters a = b = 44.780, c = 395.582 A, containing an RTP dimer within the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacillus subtilis / chemistry*
  • Bacterial Proteins*
  • Crystallization
  • Crystallography, X-Ray
  • DNA / chemistry*
  • DNA-Binding Proteins / chemistry*
  • Magnetic Resonance Spectroscopy

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • rtP protein, Bacillus subtilis
  • DNA