Published in
International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 3(69), p. 295-301, 2013
DOI: 10.1107/s1744309113002716
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Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants ofVaccinia virusuracil DNA glycosylase
,
Robert Ricciardi,
Surajit Banerjee ,
Debasish Chattopadhyay
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Abstract
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.