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EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18(NH4)2SO4 at 0.65 to 0.7% saturation 171154
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.1856500 Da domain that retains full enzymatic activity, in presence of inhibitor 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid. 2.5 A resolution, space group P212121 695355
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18best crystals grow by hanging-drop vapor diffusion by equilibrating a 1 ml drop of protein in buffer (10 mM HEPES pH 7.2, 50 mM ammonium sulfate) with 1 ml reservoir solution containing 2.0-2.5 M ammonium sulfate and suspended over 1 ml reservoir solution. Structure determined at 2.2 A resolution 677317
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides 698986
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18catalytic domain of isoform NanI, to 0.97 A resolution, and complexes with its substrate sialic acid to 0.97A resolution, with transition-state analogue 2-deoxy-2,3-dehydro-N-acetylneuraminic acid to 1.5 A resolution, and with a covalent intermediate formed using a fluorinated sialic acid analogue to 1.2 A resolution 698874
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18comparison of the catalytic cleft plasticity of free and ligand-bound forms of Trypanosoma rangeli sialidase and Trypanosoma cruzi trans-sialidase using molecular dynamics simulations. The Trypanosoma cruzi enzyme has a very flexible, widely open catalytic cleft, mostly due to resiude W312 loop motion, in apo form. In ligan-bound form, the flexibility and solvent exposure is significantly reduced. The Trypanosoma rangeli sialidase maintains a more open catalytic cleft in both apo and holo forms 696324
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18crystallization of the catalytic domain by sitting-drop vapour-diffusion. Crystals belong to space group P2(1)2(1)2(1) with unit-cell parameters a = 96.98, b = 69.41, c = 72.69 A and one monomer per asymmetric unit. The crystals diffract to at least 0.92 A 663487
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18crystallization of the enzyme alone or in complex with sialic acid, modeling 654395
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18free enzyme and in complex with N-acetylneuraminic acid or 2,3-dehydro-2-deoxy-N-acetylneuraminic acid, sitting drop vapor diffusion method, using 100 mM HEPES (pH 7.0) and 30% Jeffamine ED-2001 (pH 7.0), at 21°C 702033
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.18free enzyme, sitting drop vapor diffusion method, using 100 mM HEPES (pH 7.0), 5% tacsimate, 7% (w/v) PEG 5000MME, at 21°C 702033
Results 1 - 10 of 25 > >>