EC Number   |
|---|
    1.14.16.1 | apo DicPAH and DicPAH complexed with dihydrobiopterin (BH2) and FeIII are crystallized by the hanging-drop vapour-diffusion method. Crystals of apo DicPAH and the DicPAH-BH2-FeIII complex diffract to 2.6 and 2.07 A resolution, respectively, and belong to space group P21, with unit-cell parameters a = 70.02, b = 85.43, c = 74.86 A, beta= 110.12° and a = 70.97, b = 85.33, c = 74.89 A, beta = 110.23°, respectively |
| 1.14.16.1 | crystal structure of ternary complex of catalytic domain, Fe2+ form, with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine |
| 1.14.16.1 | crystal structure of the catalytic domain in its catalytic active Fe2+ form and as binary complex with tetrahydrobiopterin, 1.7 and 1.5 A resolution |
| 1.14.16.1 | hanging drop vapor diffusion method |
| 1.14.16.1 | hanging drop vapor diffusion method, using 0.1 M Na-HEPES, pH 7.0, 0.01 M magnesium chloride hexahydrate, 0.005 M nickel(II) chloride hexahydrate, and 15% (w/v) PEG 3350, or sitting drop vapor diffusion method, using 0.1 M Na-HEPES pH 7.0, 0.01 M magnesium chloride hexahydrate, and 15% (w/v) PEG |
| 1.14.16.1 | in complex with 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin and substrate analogues 3-(2-thienyl)-L-alanine or L-norleucine |
| 1.14.16.1 | native and selenomethyl-labelled enzyme |
| 1.14.16.1 | native enzyme by hanging drop method, 0.001 ml of protein solution containing 10 mg/ml protein in 20 mM Na-HEPES, 200 mM NaCl, pH 7.0, are mixed with 0.001 ml of reservoir solution containing 1.6-1.8 M ammonium sulfate, 100 mM NaCl, and 20 mM NaHepes, pH 7.5, equilibration at 4 °C, 3 weeks, cryoprotection with 25% glycerol, X-ray diffraction structure determination and analysis |
| 1.14.16.1 | sitting drop vapor diffusion method, using 0.1 M Bis-Tris-HCl pH 5.5, 25% (w/v) polyethylene glycol 3350, and 0.2 M magnesium chloride |
| 1.14.16.1 | vapor diffusion method, using 140 mM Na-acetate, 70 mM Na-citrate, 100 mM Na-cacodylate (pH 6.5), and 31.5% (w/v) PEG 1000 |
