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Structure reveals differences in the environment of catalytic residue Cys195 crystals grown by vapor diffusion method in hanging drop setup - hanging-drop vapour diffusion method V3L, V3F and V3Y mutant enzymes, hanging drop vapor diffusion method, using 100 mM Tris-base, pH 8.5, 20 mM 2-mercaptoethanol, 32-40% (w/v) ammonium sulfate and 16-24% (w/v) polyethylene glycol 4000 - F59A crucial dimer interface residue K47A mutation at dimer interface L198A crucial dimer interface residue L198P the mutant enzyme displays a kcat value of 2fold lower than wild type M190E the mutant enzyme displays a kcat value of 5.9fold lower than wild type W182A mutation causes an overall blue shift of the protein fluorescence emission spectrum Y202A crucial dimer interface residue, activity similar to wild-type A17T/D116A/D254E - the mutant shows decreased sensitivity towards 5-fluorodeoxyuridine compared to the wild type enzyme A191K - the mutant exhibits about 25% of the catalytic activity of the wild type enzyme

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