EC Number   |
|---|
   1.8.2.2 | purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.003 ml of 8 mg/ml protein in 20 mM Bis-Tris-HCl, pH 6.5, with 0.0015 ml of reservoir solution containing 23.5% w/v PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Bis-Tris, pH 6.28, and 0.1 M NaI, and equilibration against 0.120 ml of reservoir solution, 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.98 A resolution. The protein crystallized in space group C2 with one molecule in the asymmetric unit. Initial crystallization trials renders multiple, urchin-like crystals with no diffraction ability. Using iodide as an additive significantly improves the X-ray diffraction quality of the crystals |
| 1.8.2.2 | purified recombinant wild-type and K208N and K208G mutant enzymes, freeor in complex with tetrathionate, dithionite, or bisulfit, sitting drop vapour diffusion method, mixing of 0.003 ml of 8 mg/ml protein in 20 mM Bis-Tris-HCl, pH 6.5, with 0.0015 ml of reservoir solution containing 23.5% w/v PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Bis-Tris, pH 6.28, and 0.1 M NaI, and equilibration against 0.120 ml of reservoir solution, the complex crystals are formed by soaking in an excess of ligands, tetrathionate, dithionite, and bisulfite, 20°C, X-ray diffraction structure determination and analysis at 1.40-1.98 A resolution, modelling |
| 1.8.2.2 | three-dimensional structure of the fusion protein with electron-transferring protein TsdB, to 2.75 A resolution. In the oxidized state, the tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Thiosulfate is covalently bound to Cys330 on heme 3 |
