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Results 1 - 7 of 7
EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.7.1.145Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.145crystal structure determination, PDB IDs 1OE0, 1OT3, 1J90, 1ZM7, 1ZMX, 2JCS, 2VP0, 2VP2, 2VP4, 2VP, 2VP6, 2VP9, 2VPP, 2VQ, and 2JJ8 738781
Show all pathways known for 2.7.1.145Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.145crystals of a C-terminally truncated (D20) recombinant Dm-dNK mutant E52D are grown using the vapour diffusion method by hanging drop geometry. The E52D mutant is crystallized with its feedback inhibitor dTTP. The backbone conformation remains unchanged, and coordination between D52 and the dTTP–Mg complex is observed 673584
Show all pathways known for 2.7.1.145Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.145in complex with floxuridine, brivudine, zidovudine, zalcitabine, or dCTP or dGTP with resolution of 2.2-2.9 A. dCTP and dGTP bind with the base in the substrate site, similarly to feedback inhibitor dTTP. Contrary to nucleoside analogs, dGTP adopts a syn conformation 692289
Show all pathways known for 2.7.1.145Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.145purified recombinant enzyme in complex with dT and dTPP, hanging drop vapour diffusion method, enzyme solution containing 5-10 mg/ml protein, 5 mM dT or dTTP, is mixed in equal volumes with cyrstallization solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 18-22% w/v PEG 5000 monomethylether, and 5-10% w/v PEG 400, 3-5 days, 14°C, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution 661072
Show all pathways known for 2.7.1.145Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.145purified recombinant enzyme, hanging drop vapour diffusion method, enzyme solution containing 10 mg/ml protein and 10 mM deoxycytidine, mixed with an equal volume of cyrstallization solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 20% w/v PEG 5000, and 8-10% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement method 662932
Show all pathways known for 2.7.1.145Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.145purified recombinant mutant N64D in complex with dT or dTTP, counter diffusion and vapour diffusion methods, 20 mg/ml enzyme with 10 mM dT, is mixed with cyrstallization solution containing 0.15 M MES, pH 6.5, 0.3 M lithium sulfate, and 27,5% w/v PEG 2000 monomethylether, or 10 mg/ml enzyme with 5 mM dTTP is mixed with 0.1 M MES, pH 6.5, 0.16 M lithium sulfate, and 25% v/v PEG 2000 monomethylether, 2 weeks, 15°C, X-ray diffraction structure determination and analysis at 3.1 A and 2.2 A resolution, respectively 661702
Show all pathways known for 2.7.1.145Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.145truncated dNK lacking the last 20 amino acid residues in complex with gemcitabine, hanging drop vapor diffusion method, using 0.1 M MES pH 6.5, 0.2 M lithium sulfate and 26% (w/v) mPEG2000 702047
Results 1 - 7 of 7