EC Number |
---|
5.3.4.1 | - |
5.3.4.1 | crystal structure of reduced and oxidized enzyme |
5.3.4.1 | ERp57 and its isolated bb' and b' domains in complex with the lectin chaperone calnexin, hanging drop vapour diffusion method, equilibration of 14 mg/ml protein in 50 mM Tris-HCl, 0.15 M NaCl, 1 mM DTT, pH 7.5, against 30% w/v PEG 3350, 0.1 M (NH4)2SO4, 0.1 M HEPES buffer, pH 7.5, for 1-3 days at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resoution |
5.3.4.1 | hanging drop vapor diffusion method, using 0.01 M zinc chloride, 20% (w/v) polyethylene glycol 6000, and 0.1 M Tris-HCl (pH 8.0) |
5.3.4.1 | hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350 |
5.3.4.1 | hanging drop vapor diffusion method, using 24% (w/v) PEG 4000, 100 mM sodium acetate, pH 6.4, 25 mM sodium citrate, pH 6.4, and 17% (v/v) glycerol |
5.3.4.1 | hanging-drop vapour-diffusion, mixing of 0.003 ml protein solution i.e. 15 mg/ml protein, 25 mM HEPES, pH 7.5 with 0.003 mL reservoir solution containing 20-23% polyethylene glycol 5000, 200 mM ammonium acetate, 100 mM HEPES, pH 7.5 and 5% glycerol |
5.3.4.1 | in complex with alpha-synuclein, using 0.1 M HEPES buffer (pH 7.5) containing 25% (w/v) PEG3350 |
5.3.4.1 | molecular modeling offers a role for the conserved residue R103 in coordinating the oxidative transition-state complex |
5.3.4.1 | purified native and selenomethionine-labeled DsbG in oxidized and in redox-mixed state, DsbG is oxidized by 1.7 mM (1,10-phenanthroline)Cu(II), crystallization in 20% PEG 4000, 0.1 M sodium citrate, pH 3.8-4.2, and 0.2 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution |