EC Number |
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2.3.1.180 | 15 mg/ml purified enzyme in 20 mM Tris, pH 8.0, 3 mM DTT, 100 mM NaCl, 10% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution |
2.3.1.180 | apoenzyme or mutant enzymes C155A, C264A and C155A/C264A in complex with octanoyl-CoA, using PEG3350 as a precipitant and Tris HCl buffer (pH 7.0-8.0) and 0.1 M calcium acetate |
2.3.1.180 | crystallization of the mtFabH/decyl-CoA disulfide is achieved using the hanging-drop vapour-diffusion technique. The active site cysteine in both subunits of the wild type mtFabH dimer is able to react with either a dodecanoyl-CoA substrate or a decyl-CoA disulfide inhibitor |
2.3.1.180 | cyrstals of ecFabH and the ecFabH/methyl-CoA disulfide complex are obtained by the hanging drop method |
2.3.1.180 | enzyme in complex with inhibitor CoA methyldisulfide |
2.3.1.180 | hanging-drop vapor diffusion method, crystal structures of mtFabH and C112A mtFabH with 1 |
2.3.1.180 | mapping of the Thr45 phosphorylation site on the mtFabH crystal structure, overview |
2.3.1.180 | purified FabH as apoenzyme or ligand-bound complex, X-ray diffraction structure determination and analysis at 1.46 A resolution |
2.3.1.180 | purified FabH as apoenzyme or with bound acetyl-CoA, structure and reaction mechanism modeling |
2.3.1.180 | purified FabH, sitting drop vapour diffusion method, 2 crystal forms |