Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage

J Biochem. 2000 Jan;127(1):9-11. doi: 10.1093/oxfordjournals.jbchem.a022588.

Abstract

MutM protein, which removes the oxidatively damaged DNA base product, 8-oxoguanine (GO), has been crystallized by means of a hanging-drop vapor-diffusion procedure using polyethyleneglycol monomethylether 2000 as a precipitant in 2-(cyclohexylamino) ethanesulfonic acid (CHES) buffer, pH 9.8. The diffraction data derived from oscillation photographs indicate that the crystals belong to the monoclinic system and space group P2(1). The crystals have unit-cell dimensions of a = 45.4 A, b = 62.0 A, c = 99.7 A, and beta = 90.8 degrees. Assuming that the asymmetric unit contains two molecules, the Vm value was calculated to be 2.35 A(3).Da(-1). The crystals diffracted X-rays to at least 2.1 A resolution and were suitable for high-resolution X-ray crystal structure determination.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • DNA Damage*
  • DNA Repair*
  • DNA-Formamidopyrimidine Glycosylase
  • N-Glycosyl Hydrolases / chemistry*
  • N-Glycosyl Hydrolases / isolation & purification
  • N-Glycosyl Hydrolases / metabolism*
  • Oxidative Stress*
  • Thermus thermophilus / enzymology*

Substances

  • N-Glycosyl Hydrolases
  • DNA-Formamidopyrimidine Glycosylase