Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua).
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).
Leiros
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I
Department of Chemistry, Faculty of Science, University of Tromsø, N-9037 Tromsø, Norway.
Lanes
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O
Sundheim
O
O
Helland
R
R
Smalås
A O
AO
Willassen
N P
NP
D000818:Animals; D002816:Chordata, Nonvertebrate / Q000201:enzymology*; D003081:Cold Climate; D003460:Crystallization; D018360:Crystallography, X-Ray; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases / Q000737:chemistry*; D011487:Protein Conformation; D051981:Uracil-DNA Glycosidase
D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases; D051981:Uracil-DNA Glycosidase