Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase

Academic Article


  • Amino-acid residues located at a highly flexible area in the uracil DNA glycosylase of Vaccinia virus were mutated. In the crystal structure of wild-type D4 these residues lie at the dimer interface. Specifically, three mutants were generated: (i) residue Arg167 was replaced with an alanine (R167AD4), (ii) residues Glu171, Ser172 and Pro173 were substituted with three glycine residues (3GD4) and (iii) residues Glu171 and Ser172 were deleted (Δ171-172D4). Mutant proteins were expressed, purified and crystallized in order to investigate the effects of these mutations on the structure of the protein. © 2013 International Union of Crystallography All rights reserved.
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    Author List

  • Sartmatova D; Nash T; Schormann N; Nuth M; Ricciardi R; Banerjee S; Chattopadhyay D
  • Start Page

  • 295
  • End Page

  • 301
  • Volume

  • 69
  • Issue

  • 3