Crystallization and preliminary X-ray analysis of the uracil-DNA glycosylase DNA repair enzyme from herpes simplex virus type 1.
A 28.5 kDa catalytic fragment of the uracil-DNA glycosylase DNA repair enzyme from Herpes simplex virus type 1 (HSV-1) has been crystallized using protein from a highly expressing Escherichia coli clone of the Herpes simplex virus type 1 UL2 gene. The protein crystallizes at 12 mg/ml from 11% (w/v) polyethylene glycol 8000 at pH values in the range 6.8 to 7.0, in the presence of (NH4)2SO4. Long trigonal rods (0.08 mm x 0.08 mm x > 0.5 mm) diffract beyond 3.0 A using a laboratory source. The enzyme crystallizes in P3(1) (or P3(2)) a = 65.3 A, c = 49.0 A with a single molecule in the asymmetric unit and an estimated solvent content of 41% by volume.
Savva
R
R
Department of Biochemistry and Molecular Biology, University College London, U.K.
Pearl
L H
LH
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D045647:DNA Glycosylases; D004260:DNA Repair; D004926:Escherichia coli; D005814:Genes, Viral; D018259:Herpesvirus 1, Human / Q000201:enzymology*; D009699:N-Glycosyl Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D051981:Uracil-DNA Glycosidase
D011994:Recombinant Proteins; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases; D051981:Uracil-DNA Glycosidase