EC Number   |
|---|
    1.11.1.6 | - |
| 1.11.1.6 | ammonium sulfate precipitation |
| 1.11.1.6 | comparison with catalase from Aliivibrio salmonicida LFI1238. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. Compared with Proteus mirabilis, the four C-terminal alpha-helices of Aliivibrio salmonicida LFI1238 catalase are displaced in the structures, explaining the reduced thermal stability |
| 1.11.1.6 | diffraction to 1.96 A. Comparison with catalase from Proteus mirabilis. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. The reduced thermal stability of cold-adapted Aliivibrio salmonicida catalase may be explained by a reduced number of ion-pair networks and displacement of the four C-terminal alpha-helices |
| 1.11.1.6 | fee enzyme and enzyme complexed with ammonia or NO, hanging drop vapor diffusion method, mixing of 0.004 ml of 12-13 mg/ml protein, containing NH4OH, with an equal volume of the reservoir solution consisting of 45-60 mM magnesium formate, pH 6.7, 2-3 weeks, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.88-1.99 A resolution |
| 1.11.1.6 | hanging drop vapour diffusion method, using 24% (w/v) PEG 2000, 10 mM NaCl, 10 mM CaCl2, and 3% (w/v) 6-aminocaproic acid in 100 mM bis-Tris buffer pH 6.5 at 18°C |
| 1.11.1.6 | hanging-drop vapor diffusion method. Crystal structure of the complex of the catalase with the classical catalase inhibitor 3-amino-1,2,4-triazole is determined at 1.95 A resolution |
| 1.11.1.6 | homology modeling using crystal structures of human and bovine catalases |
| 1.11.1.6 | metal-bound [FeII/FeII]-ADEec and [FeII/MnII]-ADEec enzyme, sitting drop vapor diffusion, room temperature, X-ray diffraction struccture determination and analysis at 2.63-2.8 A resolution |
| 1.11.1.6 | mutant M244A, diffraction to 2.0 A, monoclinic space group C2, presence of a dimer in the asymmetric unit |
