EC Number |
---|
4.3.1.17 | - |
4.3.1.17 | crystal structure obtained by molecular replacement shows a homodimer and a fold typical for beta-family pyridoxal 5'-phosphate-dependent enzymes. Each monomer serves as an active unit |
4.3.1.17 | crystal structures of apo-SDH and holo-SDH, crystallized with O-methylserine, at 2.8 A and 2.6 A resolution, respectively |
4.3.1.17 | hanging-drop vapor-diffusion method, crystal structures of the native and 1-aminocyclopropane-1-carboxylate-complexed enzyme. The crystals of native and Se-Met belong to the space group P3(2)21 with unit cell parameters of a=b= 122.3 A, c = 115.0 A, and gamma = 120°, and there are three molecules in an asymmetric unit. The crystals of the ACC complex belong to space group P1 with unit cell parameters of a = 105.8 A, b = 147.2 A, c = 149.0 A, a = 73.18, b = 90.18, and gamma = 68.48, and 24 molecules are included in an asymmetric cell |
4.3.1.17 | hanging-drop vapour diffusion, 0.002 ml protein solution containing 20-30 mg/ml SDH in 20 mM Tris-HCl, pH 7.6 and 150 mM NaCl is mixed with 0.002 ml reservoir solution containing 800 mM ammonium sulfate in 100 mM Tris-HCl, pH 7.0-8.0, crystals diffract to 2.5 A |
4.3.1.17 | purified recombinant cSDH, hanging drop vapour diffusion method, 10 mg/ml protien in 50 mM Na-citrate, pH 5.6, 10 mM DL-O-methylserine, 200 mM potassium acetate, 5 mM dithiothreitol, 15% w/v PEG-8000 at 21°C, 1 week, X-ray diffraction structure determination and analysis at 2.8 A resolution |
4.3.1.17 | structure of A65S hSDH mutant is determined at 1.3 A resolution |
4.3.1.17 | to 1.76 A resolution. The active site is located between the small domain and large domain, and a pyridoxal 5'-phosphate is attached to Lys52 by a Schiff-base linkage |