EC Number |
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1.13.11.40 | deletion mutant of 8R-LOX crystallized by sitting drop vapor diffusion, to 1.85 A resolution, belongs to space group P21 with four molecules in the asymmetric unit. U-shaped channel in 8R-LOX |
1.13.11.40 | hanging drop vapour diffusion in 6.25% polyethylene glycol 8000, 100 mM imidazole acetate (pH 8.0), 100 mM CaCl2, and 5% sucrose at 22°C |
1.13.11.40 | molecular dynamics simulations. The enzyme is stable in both apo and substrate bound complex forms. The substrate adopts a bent structure inside the enzyme active site, with the C1 carboxylate and C20 methyl groups of the substrate at two terminal ends of the two sides, while the substrate is folded at the double allylic carbon center (C10 position) |
1.13.11.40 | purified enzyme 8R-LOX containing the arachidonate substrate in subunit C |
1.13.11.40 | purified enzyme in complex with arachidonic acid, anaerobic conditions, vapor diffusion with a well solution of 8% PEG-8000, 5% glycerol, 0.2 M CaCl2, 0.1 M imidazole acetate, pH 8.0, crystals are soaked for about 17 h in a solution consisting of 25% glycerol, 10% PEG-8000, 0.02 M CaCl2, 0.1 M imidazole acetate, pH 8.0, 1% dimethyl sulfoxide, and 1 mg/ml arachindonic acid, X-ray diffraction structure determination and analysis at 2.0 A resolution |