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EC Number Crystallization (Commentary)
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4-
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4commercial enzyme preparation at 20 mg/ml, native enzyme or complexed with inhibitor purine riboside, sitting drop vapour diffusion method, micro-stirring technique over 2 weeks, from 2.2 M ammonium sulfate, 2% 2-methyl-2,4-pentanediol, 0.1 M MES, pH 6.0, 20°C, with reservoir solution containing 20% 2-propanol, 20% PEG 4000, 0.1 M citrate, pH 5.6, X-ray diffraction structure determination and analysis at 1.8 A resolution
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4crystal structure of a surface engineered adenosine deaminase at a resolution of 2.48 A
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4crystal structure of adenosine deaminase from Plasmodium vivax in complex with inhibitor, 2’-deoxycoformycin (pentostatin), 33% PEG 20000, 0.1 M TAPS (pH 9.0), 0.1 M Sodium phosphate (monobasic), 16% acetonitrile, 5 mM adenosine, pH 7.0, vapor diffusion, sitting drop, temperature 298K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular modeling, crystal structure of adenosine deaminase from Plasmodium vivax in complex with adenosine, space group C 2 2 21, X-ray diffraction structure determination and analysis at 1.89 A resolution, crystal structure of adenosine deaminase from Plasmodium vivax in complex with guanosine, 27.3% PEG 20000, 0.1 M CHES (pH 9.5), 0.1 M Sodium phosphate monobasic, 5 mM guanosine, vapor diffusion, sitting drop, temperature 293K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.19 A resolution, these structures highlight a drastic conformational change in plasmodial adenosine deaminase upon substrate binding, these complexes illuminate the structural basis for the differential substrate specificity and potential drug selectivity between mammalian and parasite enzymes
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4crystal structure of adenosine deaminase ligated with (+)-erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), vapor diffusion, sitting drop, 2 M ammonium sulfate, 2% 2-methyl-2, 4-pentanediol, 0.1 M MES buffer, pH 6.0, temperature 293K, , X-ray diffraction structure determination and analysis at 2.52 A resolution, space group P 43 21 2, EHNA induces conformational change of adenosine deaminase to the open form in the crystalline state, structural comparison between the EHNA-ADA complex and the 1-eaza-adenosine-ADA complex
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4crystals of the complex of adenosine deaminase with 6-hydroxy-1,6-dihydropurine riboside are grown against reservoirs containing 2.0-2.2 M ammonium sulfate, 2% v/v polyethylene glycol 400 in 0.1 M HEPES buffer, pH 7.5, solved at 2.5 A resolution
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4holo- and apo-ADA, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 200 mM ammonium sulfate, pH 4.7 for apo-ADA or 25% (w/v) PEG 6000, 20 mM Tris-HCl and pH 8.5 for holo-ADA
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4molecular modeling enzyme-inhibitor, docking simulations enzyme-inhibitor, drug design
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4Plasmodium vivax ADA in a complex with 5'-methylthiocoformycin is crystallized by the sitting drop vapor diffusion method, using 25% (w/v) PEG3350, 100 mM HEPES (pH 7.5), and 0.2 M MgCl2
Show all pathways known for 3.5.4.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.4purified intestinal enzyme complexed with 1-[(R)-1-hydroxy-4-(6-(5-phenylvalerylamino)indol-1-yl)2-butyl]imidazole-4-carboxamide, 1-[(R)-1-hydroxy-4-(6-(3-phenylpropionylamino)indol-1-yl)2-butyl]imidazole-4-carboxamide, or 1-[(R)-4-(6-(3-benzylureido)indol-1-yl)-1-hydroxy-2-butyl]imidazole-4-carboxamide, protein solution is mixed with precipitant solution containing 100 mM MES, pH 6.0, 2.1 ammonium sulfate, and 2.5% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.2 A resolution
Results 1 - 10 of 11 > >>