EC Number   |
Reference |
|---|
  1.7.1.17 | docking simulations. The isoalloxazine ring of FAD localizes at the same site and plays the same role as that of FMN in AzrA |
745571 |
| 1.7.1.17 | in complex with FMN, sitting drop vapor diffusion method, using 0.17 M ammonium sulfate and 25.2% (w/v) PEG 4000 |
763801 |
| 1.7.1.17 | in complex with FMN, to 2.07 A resolution. The AzoA monomer shows a typical NAD(P)-binding Rossmann fold with a highly conserved FMN binding pocket. A salt bridge between Arg18 and Asp184 restricts the size of the flavin binding pocket such that only FMN can bind |
744155 |
| 1.7.1.17 | purified oxidized or reduced AzoR, free or in complex with inhibitor dicoumarol, hanging drop vapor diffusion method, mixing of equal volumes of 8 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 100 mM NAD+ and 0.1 mM FMN with reservoir solution containing 200 mM NaOAc, 200 mM sodium cacodylate, pH 6.7, 15% w/v PEG 8000, and 3% v/v dimethyl sulfoxide, equilibration over reservoir solution, at 25 °C, 2 weeks, X-ray diffraction structure determination and analysis at 1.4-2.3 A resolution, molecular replacement using the 1.8 Å resolution structure of oxidized AzoR as a search model, modelling |
742834 |
| 1.7.1.17 | purified recombinant enzyme, sitting drop vapour-diffusion method, mixing 0.015 ml of 23 mg/ml protein in 10 mM Tris-HCl, pH 8.0, and 1 mM FMN, with an equal volume of reservoir solution containing 200 mM MgCl2, 30% v/v 2-propanol, and 100 mM HEPES, pH 7.5, equilibration over 0.5 ml reservoir solution, one week, 15°C, method optimization, crystal soaking in heavy metal solution with K2PtCl4, X-ray diffraction structure determination and analysis at 1.8-2.5 A resolution. FMN is tightly bound to the protein moiety, and this interaction is essential for the crystallization of AzoR |
741517 |
| 1.7.1.17 | purified recombinant His-tagged wild-type enzyme in complex with FMN/N-cyclohexyl-2-aminoethanesulfonate (CHES) and Y151F enzyme mutant in complex with FMN, sitting drop vapor diffusion method, mixing of 0.002 ml of 42 mg/ml protein solution with an equal volume of reservoir solution containing 40% PEG 600 and 100 mM CHES, pH 9.5 for the wild-type, and 36% PEG 600 and 100 mM phosphate-citrate buffer, pH 4.2 for the mutant, equilibration against 0.1 m reservoir resolution, 20°C, X-ray diffraction structure determination and analysis at 1.97 and 1.95 A resolution respectively, molecular replacement method. Diffraction-quality crystals for the Y127F mutant cannot be obtained |
763965 |
| 1.7.1.17 | to 1.6 A resolution, space group F222, with unit-cell parameters a = 72.1, b = 95.5, c = 146.1 A |
743951 |
