EC Number   |
|---|
   2.1.1.77 | - |
| 2.1.1.77 | hanging drop vapor diffusion method, crystal structure at 2.8 A resolution. The monomeric structure of StoPIMT consists of two domains, an AdoMet-dependent methyltransferase fold domain and a distinctive C-terminal alpha-helical domain. Six monomers associate into a hexamer, in which there are three contact regions per monomer, referred to as the major, minor, and C-terminal alpha-helical contact regions |
| 2.1.1.77 | hanging-drop vapour diffusion. Crystal structure shows that the enzyme has a distinctive hexameric structure composed of monomers consisting of two domains and a C-terminal alpha-helical domain |
| 2.1.1.77 | in complex with S-adenosyl-L-homocysteine, hanging drop vapor diffusion method, using |
| 2.1.1.77 | in complex with S-adenosyl-L-homocysteine, hanging drop vapor diffusion method, using 0.1 M HEPES-Na [pH 7.5], 0.8 M monosodium dihydrogen phosphate, and 0.8 M monopotassium dihydrogen phosphate, at 15°C |
| 2.1.1.77 | sitting drop vapour diffusion method, resolution of 2.2 A |
