EC Number   |
|---|
   4.2.2.3 | 8 mg/ml purified isozyme A1-III complexed with trisaccharide product 4-deoxy-L-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid, hanging drop vapour diffusion method, 0.1 M HEPES, pH 7.5, containg 48% PEG w/v saturated ammonium sulfate, 290 mM trisaccharide, 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution |
| 4.2.2.3 | crystal structure at 1.77 A resolution and putative substrate-binding model. The enzyme adopts a beta-jelly roll fold at the core of the structure and residues Lys99, Tyr140, and Tyr142 form catalytic residues in the active site |
| 4.2.2.3 | crystal structures of native protein and its inactive mutant H531A in complex with alginate trisaccharide, at 2.10 and 2.99 A resolutions with final R-factors of 18.3 and 19.9%, respectively. The enzyme is comprised of an alpha/alpha-barrel plus anti-parallel beta-sheet as a basic scaffold. His311 and Tyr365 are the catalytic base and acid, respectively. A short alpha-helix in the central alpha/alpha-barrel domain and a conformational change at the interface between the central and C-terminal domains are essential for the exolytic mode of action |
| 4.2.2.3 | crystallization at 20°C by sitting-drop vapour diffusion with polyethylene glycol 4000 as a precipitant. X-ray analysis shows that the Atu3025 crystal belong to space group P2(1) and diffracted to 2.8 A resolution, with unit cell parameters a = 107.7, b = 108.3, c = 149.5 A, beta = 91.5° |
| 4.2.2.3 | hanging drop vapour diffusion method, 0.003 ml protein solution: 17.2 mg/ml protein, 0.1 M HEPES, pH 7.5, + 0.003 ml bottom solution: 47-49% saturated ammonium sulfate, 0.1 M HEPES, pH 7.5, 20°C, 1 month, for large crystals micro- and macroseeding is used, crystal are soaked in heavy-atom derivatives for 1-4 h for X-ray diffraction structure determination and analysis at 1.78-10.0 A resolution |
| 4.2.2.3 | hanging-drop vapour diffusion method, crystal structure determined at 2.0 A resolution. PA1167 forms a glove-like beta-sandwich composed of 15 beta-strands and 3 alpha-helices |
| 4.2.2.3 | hanging-drop vapour-diffusion method, 1.2 A resolution |
| 4.2.2.3 | purified isozyme A1-II, hanging drop vapour diffusion method, 0.003 ml protein solution: 38 mg/ml protein, 50 mM Tris-HCl, pH 7.5, + 0.003 ml bottom solution: 0.1 M Tris-HCl, pH 8.5, 43% saturated ammonium sulfate, 8% PEG 4000, 0.2 M Li2SO4, 20°C, 1 month, X-ray diffraction structure determination and analysis at 2.8 A resolution |
| 4.2.2.3 | purified recombinant full-length dimeric AlyA5, hanging drop vapor diffusion method, 0.002 ml of 7.7 mg/ml protein solution with 0.1 mg/ml oligoglucuronate, are mixed with 0.001 ml of reservoir solution containing PEG 3350 and 0.2 M sodium/potassium tartrate, and equilibration against 0.2 ml reservoir solution, 21°C, screening and method optimization, X-ray diffraction structure determination and analysis at 1.75 A resolution |
| 4.2.2.3 | purified recombinant His-tagged AlgL28-362 protein, hanging drop vapour diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, with 0.002 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate, pH 4.6, 28% w/v PEG 4000, 0.3 M PIPES, method optimization, 4 days, 20°C, X-ray diffraction structure determination and analysis at 1.64 A resolution |
