EC Number |
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3.2.1.91 | - |
3.2.1.91 | by 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 |
3.2.1.91 | D416A mutant, hanging drop vapor diffusion method, complexed with methyl cellobiosyl-4-thio-beta-cellobioside |
3.2.1.91 | engineered enzymes |
3.2.1.91 | hanging drop vapor diffusion method |
3.2.1.91 | hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M HEPES pH 7.0, 0.14 M lithium chloride |
3.2.1.91 | hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M sodium citrate (pH 4.0) and 1 M lithium chloride |
3.2.1.91 | microbatch and hanging drop vapour diffusion methods with 16.25% PEG 8000, 0.05 M sodium acetate pH 4.5, 0.12 M Li2SO4 |
3.2.1.91 | molecular 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 |
3.2.1.91 | purified 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 |