EC Number |
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3.1.4.12 | apo-enzyme and in complex with phosphorylcholine, hanging drop vapor diffusion method, using 0.2 M NH4NO3 and 25% (w/v) PEG 3350 |
3.1.4.12 | catalytic domain in complex with CMP, sitting drop vapor diffusion method, using 2.08 M disodium malonate pH 5, 0.23 M sodium thiocyanate |
3.1.4.12 | hanging drop vapor diffusion method, crystal structures of Bc-SMase complexed to the functional metal ions Mg2+, Co2+, or Ca2+ are determined at 1.8 A, 1.8 A, and 1.4 A resolution, respectively |
3.1.4.12 | hanging-drop vapor diffusion method, 1.9 A resolution |
3.1.4.12 | hanging-drop vapour-diffusion method, single crystals with dimensions 0.2 * 0.2 * 0.4 mm are obtained, diffraction data are collected to 1.8 A under cryogenic conditions, space group P6 with unit-cell parameters a = b = 140.6 A, c = 113.6 A |
3.1.4.12 | in complex with phosphocholine, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 as precipitant |
3.1.4.12 | nSMase, crystal structure and structure-function analysis |
3.1.4.12 | nSMase, crystal structure of nSMase complexed with Ca2+, Co2+, or Mg2+, and structure-function analysis |
3.1.4.12 | purified recombinant mutant N57A enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH7.0, with 0.002 ml of reservoir solution containing 18% w/v PEG 8000, 0.2 M MgCl2, and 0.1 M sodium cacodylate, pH 6.5, 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution |
3.1.4.12 | purified wild-type enzyme and L-selenomethionine-labeled enzyme, mixing of 0.002 ml of 1.5 mg/ml protein in 50 mM Tris, pH 7.4, 50 mM NaCl, and 0.1 mM TCEP, with 700 nl of reservoir solution containing 10% dioxane, 0.1 M MES, pH 6.75 and 1.5 M ammonium sulfate, and 300 nl 0f 300 mM zwittergent solution, for the labeled enzyme, a protein solution at 9 mg/ml in 50 mM Tris, pH 7.4, 50 mM NaCl, and 0.1 mM TCEP is used, X-ray diffraction structure determination and analysis at 4.0 A and 2.75 A resolution, respectively, molecular replacement |