Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua)

Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1706-8. doi: 10.1107/s0907444901013427. Epub 2001 Oct 25.


Uracil-DNA glycosylase (UDG) is a DNA-repair enzyme involved in the removal of uracil from DNA. The Atlantic cod UDG (cUDG) possesses typical cold-adaptation features, with higher catalytic efficiency and lower thermal stability than the mammalian counterparts. cUDG has been crystallized by the vapour-diffusion method using sodium citrate as the precipitant at pH 7.5. The crystals are monoclinic and belong to space group P2(1), with unit-cell parameters a = 68.58, b = 67.19, c = 68.64 A, beta = 119.85 degrees. There are two molecules in the asymmetric unit, with a corresponding V(M) value of 2.71 A(3) Da(-1) and a solvent content of 54.7%. Synchrotron diffraction data have been collected to 1.9 A resolution using cryogenic conditions (120 K).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chordata, Nonvertebrate / enzymology*
  • Cold Climate
  • Crystallization
  • Crystallography, X-Ray
  • DNA Glycosylases*
  • N-Glycosyl Hydrolases / chemistry*
  • Protein Conformation
  • Uracil-DNA Glycosidase


  • DNA Glycosylases
  • N-Glycosyl Hydrolases
  • Uracil-DNA Glycosidase

Associated data

  • PDB/1AKZ