   2.7.3.4 | purified recombinant wild-type and mutant enzymes complexed with taurocyamine or L-arginine, sitting drop vapor diffusion method, mixing of 5 mg/ml protein in 20mM Tris-HCl, pH 8.5, with reservoir solution, containing 200mM diammonium tartrate, pH 5.4, 20% w/v PEG 3350, 20% v/v ethylene glycol, in a 2:1 or 1:1 protein/solution volume ratio, 2 weeks, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution leads to a small angle x-ray scattering model of SmTK-TSA in solution with two closed active sites, molecular replacement. The SmTK crystal is soaked with the dead end transition state analogue components taurocyamine-NO3 2-MgADP |
738646 |
| 2.7.3.4 | sitting-drop vapour-diffusion, 100 mM MES, pH 6.5, 25%(w/v) PEG 3000, 290 K, unit-cell parameters a = 52.7, b = 122.1, c = 63.2 A , beta = 108.5°, space group P21, 2.8 A resolution on ESRF beamline ID29 |
690293 |
