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

Citation
I. Leiros et al., Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua), ACT CRYST D, 57, 2001, pp. 1706-1708
Citations number
17
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
11
Pages
1706 - 1708
Database
ISI
SICI code
0907-4449(200111)57:<1706:CAPXDA>2.0.ZU;2-I
Abstract
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-ada ptation features, with higher catalytic efficiency and lower thermal stabil ity than the mammalian counterparts. cUDG has been crystallized by the vapo ur-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 par ameters a = 68.58, b = 67.19, c = 68.64 Angstrom, B = 119.85 degrees. There are two molecules in the asymmetric unit, with a corresponding V-M value o f 2.71 Angstrom (3) Da(-1) and a solvent content of 54.7%. Synchrotron diff raction data have been collected to 1.9 Angstrom resolution using cryogenic conditions (120 K).