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EC Number
Crystallization
Reference
crystal structure determination and analysis
purified recombinant enzyme in both its iron-free and iron-bound forms or with bound substrate, and of mutants Y122F and F86Y/F87Y, sitting drop vapor diffusion method, from reservoir solution of 0.2 mol/l Mg2+, 0.1 mol/l Tris, pH 8.5, 30% w/v PEG 4000, for the iron-bound crystals, 4 mM ferrous ammonium sulfate is added to SeADO protein solutions right before crystallization, and for the substrate-bound enzyme, 0.2mol/l L-proline, 0.1mol/l HEPES, pH 7.1, 25% w/v PEG 1500 is used, 18°C, X-ray diffraction structure determination and analysis at 1.71-2.9 A resolution
purified recombinant wild-type and mutant L194A in complex with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal, trans-2-nonylcyclopropane-1-carboxylic acid, or stearate, X-ray diffraction structure determination and analysis at 1.60-2.21 A resolution. It appears that the fatty acids are necessary for crystallization. Attempts to crystallize the enzyme in fully metalated form by including Fe2+ or Zn2+ ions in the crystallization buffer together with 11-(2-(2-ethoxyethoxy)ethoxy)undecanal are unsuccessful
Results 1 - 3 of 3