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Results 1 - 10 of 10
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6- 23605, 35234, 35238
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6hanging drop vapor diffusion method, using 170 mM ammonium sulfate, 28% (w/v) PEG 4000, 5% (v/v) glycerol and 0.5% (w/v) n-octyl-beta-D-glucopyranoside 750537
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6hanging drop vapor diffusion method, using 20% (w/v) PEG-3000, 0.1 M HEPES pH 7.5, 0.2 M NaCl (selenomethionine-substituted enzyme) or nanodrop vapor diffusion method, using 0.2 M calcium acetate hydrate, 20% (w/v) PEG 3350, pH 7.3 at 20°C (native enzyme) 730907
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6His-tagged protein, both in the native form and with selenomethionine substitution 663520
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6molecular dynamic simulations and automated docking with R and S enantiomers of substrate 1,1,1-trifluoro-2-phenyl-but-3-yn-1-yl acetate using structure of wild-type and structural model of double mutant E188W/M193C, S enantiomer fits better in active site of mutant E188W/M193C because subtrates phenyl group points out of it, docking of the preferred R enantiomer by the wild-type with lower free energy than docking of the S enantiomer 695582
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6purified selenomethionine enzyme, 6-7 mg/ml, pure or complexed with the inhibitor dimethylarsinic acid, crystal growth in 1.8 M ammonium sulfate, 0.1 M NaCl, 0.1 M cacodylate, pH 6.5, for crystallization of native methionine enzyme 1.7 M ammonium sulfate, 0.1 M NaCl, 0.1 M BES, pH 6.4, is used, X-ray structure determination and analysis at 1.3 A and 1.45 A resolution 652394
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6S10A mutant enzyme complexed with an acetate ion, sitting drop vapor diffusion method, using 0.1 M MES buffer (pH 6.5), 15-20% (v/v) PEGME 550, and 10 mM ZnSO4 749806
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6structural modelling using Cn3D 4.1 software and plant strictosidine synthase as model structure, six-bladed beta-propeller structure 696095
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6structural superimposition of homology-generated model with Alicyclobacillus acidocaldarius EST2 and Escherichia coli beta-cystathionase MalY revealed nine amino acid consensus sequence putatively involved in protein-protein interactions, amino acids 178-184 are putative core of interaction with MalY and MalT 701087
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.6using 0.2 M ammonium phosphate (pH 4.6), and 20% (w/v) polyethylene glycol 3350 750541
Results 1 - 10 of 10