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EC Number Crystallization (Commentary)
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91-
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91by the hanging-drop vapour-diffusion method, to 1.6 A resolution. Square prismatic crystal belongs to the triclinic space group P1, with unit-cell parameters a=44.04, b=45.11, c=48.90 A, alpha=77.81, beta=87.34, gamma=68.79
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91D416A mutant, hanging drop vapor diffusion method, complexed with methyl cellobiosyl-4-thio-beta-cellobioside
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91engineered enzymes
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91hanging drop vapor diffusion method
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M HEPES pH 7.0, 0.14 M lithium chloride
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M sodium citrate (pH 4.0) and 1 M lithium chloride
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91microbatch and hanging drop vapour diffusion methods with 16.25% PEG 8000, 0.05 M sodium acetate pH 4.5, 0.12 M Li2SO4
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91molecular docking of different ligands from D-glucose and beta-cellobiose through beta-cellohexaose in various combinations of subsites -4 through +4. Subsite -2 binds glucose more strongly than do subsites-1 and +1. Ligands with their nonreducing-end glucosyl residues located in subsite -2 have more negative intermolecular energy values than corresponding ligands docked elsewhere. Subsites -4, -3, +3, and +4 are less important
Show all pathways known for 3.2.1.91Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.91purified catalytic modules of wild-type enzyme Cel7A and mutants E212Q and E217Q in complex with xylooligosaccharides, hanging drop vapor diffusion method, mixing of equal volumes of 6 mg/ml protein in 10 mM sodium acetate, pH 5.0, with reservoir solution containing 20% PEG 5000 monomethyl ether, 0.1 M MES, pH 6.0, 10 mM CoCl2, and 12.5% glycerol, microseeding, 1-2 days, X-ray diffraction structure determination and analysis at 1.42-1.89 A resolution, structure modelling. Each structure model contains all 434 amino acid residues of the HjeCel7A catalytic module, with an N-terminal pyroglutamate residue and an N-acetyl glucosamine residue bound to Asn270
Results 1 - 10 of 12 > >>