Preliminary crystallographic study of Escherichia coli RuvC protein. An endonuclease specific for Holliday junctions

J Mol Biol. 1994 Aug 12;241(2):281-2. doi: 10.1006/jmbi.1994.1500.

Abstract

Single crystals of the RuvC protein, an Escherichia coli endonuclease specific for Holliday junctions, were grown by the microdialysis method. The crystals belong to the space group P2(1), with unit cell dimensions a = 72.8 A, b = 139.6 A, c = 32.4 A and beta = 93.0 degrees, and contain four molecules in an asymmetric unit. Diffraction data to a Bragg spacing of 2.5 A resolution has been obtained using a synchrotron X-ray source.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • DNA Repair / genetics
  • Endodeoxyribonucleases / chemistry*
  • Endodeoxyribonucleases / genetics
  • Endodeoxyribonucleases / isolation & purification
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Recombination, Genetic

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • ruvC protein, E coli
  • Endodeoxyribonucleases