EC Number |
Reference |
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3.2.1.143 | crystallization of ADP-ribose bound wild-type enzyme and mutant enzymes T267K and T267R, X-ray diffraction structure determination and analysis at 1.97 A resolution, monoclinic crystals with space group P21 |
754824 |
3.2.1.143 | enzyme catalytic domain free or in complexes with ADP-ribose and inhibitor ADP-HPD, as well as four enzyme catalytic residues mutants, X-ray diffraction structure determination and analysis |
732776 |
3.2.1.143 | in complexes with ADP-ribose and inhibitor adenosine 5'-diphosphate (hydroxymethyl) pyrrolidinediol |
716339 |
3.2.1.143 | purified ARH3-ADPR substrate complex, sitting drop vapour diffusion method, ARH3 and ADPR are mixed in the molar ratio of 1:3, mixing of equal volumes of 11 mg/ml protein complex in 10 mM Tris-HCl, pH 8.0, and 100 mM NaCl with reservoir solution consisting of 0.1 M MES, pH 6.0, and 20% w/v PEG MME 2000, addition of 0.2 M non-detergent sulfobetaine NDSB-201, 20°C, X-ray diffraction structure determination and analysis at 1.58 A resolution, molecular replacement using the structure of apo-ARH3 (PDB ID 2FOZ) as the search model, modeling |
754168 |
3.2.1.143 | purified enzyme in complex with ADP-ribose dimer, X-ray diffraction structure determination and analysis at 1.9 A resolution |
753967 |
3.2.1.143 | purified recombinant full-length ARH3 wild-type enzyme and D314E mutant in complex with ADP-ribose and Mg2+, hanging drop vapor diffusion method, 10 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1 mM DTT, and 5% glycerol, is mixed with reservoir solution containing 22% PEG 4000, 0.1 M sodium acetate, pH 4.5, and 0.1 M MgSO4, at 22°C, crystals are briefly equilibrated in a harvesting solution containing 26% PEG 4000, 0.1 M sodium acetate, pH 4.5, 0.1 M MgSO4, and 5 mM ADP-ribose, transferred to a cryoprotectant solution (26% PEG 4000, 0.1 M sodium acetate, pH 4.5, 0.1 M MgSO4, 5 mM ADPR, and 15% glycerol), and then flash-cooled in liquid nitrogen for data collection, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution, molecular replacement using the apo-ARH3DELTAN16 structure as a search model |
754165 |
3.2.1.143 | purified recombinant His-tagged enzyme in complex with ADP-ribose or inhibitor RBPI-3, and as selenomethionine-labeled enzyme, sitting drop vapour diffusion method, 15 mg/ml protein is mixed with a 1:1 molar ratio with ADP-ribose, and with an equal volume of a solution containing 0.15 M potassium thiocyanate, 0.1 M Tris, pH 8.5, and 15% PEG 6000, or with 0.2 M potassium bromide, 0.1 M Tris, pH 7.5, and 15% PEG 4000, X-ray diffraction structure determination and analysis at 1.95 A resolution |
732568 |
3.2.1.143 | purified recombinant mutant K616A/Q617A/K618A/E688A/K689A/K690A, also in selenomethionine-labeld form, in complex with inhibitors, sitting drop vapour diffusion, mixing protein in SEC buffer at 7.5 mg/mL with a precipitant consisting of 28% PEG 3350, 0.2 M magnesium chloride, 0.1 M PCTP (0.04 M sodium propionate, 0.02 M sodium cacodylate, 0.04 M Bis-Tris propane), pH 7.5, in a 1:1 ratio to give a 0.004 ml drop, 20°C, X-ray diffraction structure determination and analysis at 1.75-1.83 A resolution, molecular replacement |
732714 |
3.2.1.143 | purified truncated native and selenomethionine-labeled enzymes comprising residues 385-972 and lacking the A-domain, free or in complex with adenosine diphosphate (hydroxymethyl) pyrrolidinediol, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 5% glycerol and 2 mM DTT, with an equal volume of well solution containing 16-20% w/v PEG 2000 monomethylether, 0.1 M Tris-HCl, pH 7.5, 0.1 M NaCl, and 0.2 M potassium thiocyanate, 22°C, X-ray diffraction structure determination and analysis at 1.95 A resolution |
732567 |
3.2.1.143 | reaction mechanism modelling on crystal structure PDB ID 3SIG |
732351 |