Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt 7):582-5. doi: 10.1107/S174430910702622X. Epub 2007 Jun 11.

Abstract

EcoR124I is a multicomplex enzyme belonging to the type I restriction-modification system from Escherichia coli. Although EcoR124I has been extensively characterized biochemically, there is no direct structural information available about particular subunits. HsdR is a motor subunit that is responsible for ATP hydrolysis, DNA translocation and cleavage of the DNA substrate recognized by the complex. Recombinant HsdR subunit was crystallized using the sitting-drop vapour-diffusion method. Crystals belong to the primitive monoclinic space group, with unit-cell parameters a = 85.75, b = 124.71, c = 128.37 A, beta = 108.14 degrees. Native data were collected to 2.6 A resolution at the X12 beamline of EMBL Hamburg.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray / methods
  • Deoxyribonucleases, Type I Site-Specific / chemistry*
  • Deoxyribonucleases, Type I Site-Specific / isolation & purification
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / isolation & purification

Substances

  • Escherichia coli Proteins
  • endodeoxyribonuclease EcoR124I
  • Deoxyribonucleases, Type I Site-Specific
  • HsdR protein, E coli