Crystallization and preliminary X-ray analysis of RecG, a replication-fork reversal helicase from Thermotoga maritima complexed with a three-way DNA junction

Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1695-6. doi: 10.1107/s0907444901013105. Epub 2001 Oct 25.

Abstract

The monomeric 3'-5' helicase RecG from the thermophilic bacterium Thermotoga maritima has been crystallized in complex with a three-way DNA junction, the preferred physiological substrate. The crystals were obtained by hanging-drop vapour diffusion. The crystals belong to space group C2, with unit-cell parameters a = 133.7, b = 144.6, c = 84.0 A, beta = 113.8 degrees. Native data to a resolution of 3.25 A were collected from crystals flash-cooled to 100 K.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • DNA / chemistry*
  • DNA / metabolism
  • Escherichia coli Proteins*
  • Nucleic Acid Conformation
  • Protein Conformation
  • Thermotoga maritima / enzymology*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • RecG protein, E coli
  • DNA