   3.4.22.36 | active forms of caspase-1 bound to the active-site inhibitors Ac-WEHD-CHO and z-Val-Ala-Asp-fluoromethylketone, or active-site ligand-free enzyme, the active-site ligand-free and allosterically inhibited conformations are nearly identical, hanging-drop vapor diffusion at 4°C against a reservoir containing for mutant R286K: 0.1 M 1,4-piperazinediethanesulfonic acid, pH 6.0, 200 mM Li2SO4, 25% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl2, or for mutant E390D: 0.1 M Pipes, pH 6.0, 350 mM (NH4)2SO4, 20% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl2, or for mutant R286K/E390D: 0.1 M Pipes, pH 6.0, 175 mM (NH4)2SO4, 20% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl, X-ray diffraction structure determination and analysis at 1.8-2.1 A resolution, molecular replacement |
| 3.4.22.36 | enzyme mutants in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid, hanging drop vapor diffusion method, using 0.1 M PIPES pH 6.0, 75-175 mM (NH4)2SO4, 25% (w/v) PEG 2000 MME, 10 mM dithiothreitol, 3 mM NaN3, and 2 mM MgCl2 |
