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Results 1 - 6 of 6
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.96at 1.9 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.96CBM32 (a family 32 carbohydrate-binding module of endo-beta-1,4-N-acetylglucosamidase), hanging drop vapor diffusion method, using 30% (w/v) PEG 4000, 0.2 M ammonium acetate and 0.1 M sodium citrate pH 6.5
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.96Endo-A in the native form or in complex with Man3GlcNAc-thiazoline or GlcNAc-Asn, between 2-3.5 A resolution. Crystals of Endo-A belong to P1 space group with four molecules of the protein in the asymmetric unit. The carbohydrate moiety sits above the TIM-barrel in a cleft region surrounded by aromatic residues. N171 is hydrogen bonded to the thiazoline nitrogen, mimicking the ability of the asparagine to orient the acetamido group for a nucleophilic attack on the anomeric carbon
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.96hanging drop vapor diffusion method, complexed with Gal-beta(1-4)-GlcNAc-beta(1-2)-Man-alpha(1-3)[Gal-beta(1-4)-GlcNAc-beta(1-2)-Man-alpha(1-6)]Man-beta(1-4)-GlcNAc
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.96purifed recombinant wild-type enzyme and mutant E173Q in unlabeled or selenomethionine-labeled forms, 1:1 mixture of 42 mg/mL protein with a reservoir solution consisting of 0.35 M KSCN, 0.1 M 1,3-bis(tris(hydroxymethyl)methylamino)propane, pH 6.5, and 15% w/v PEG 3350, 30 days at 4 °C for the unlabeled, and 14 days at 18 °C for the SeM-labeled enzymes, X-ray diffraction and analysis at 1.8 A resolution, multiple-wavelength anomalous scattering methods, structure modelling, overview
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.96wild-type enzyme and mutant enzymes D130N, D130E, D130A, E132Q, E132A, and D130N/E132Q
Results 1 - 6 of 6