EC Number   |
|---|
   3.4.21.64 | - |
| 3.4.21.64 | at 0.15 nm resolution |
| 3.4.21.64 | at 1.5 A resolution |
| 3.4.21.64 | at 3.3 A resolution |
| 3.4.21.64 | computer modeling studies indicates the presence of a small binding pocket in the vicinity of the proteinase K active site, which may be filled by the aromatic phenylalanine moiety |
| 3.4.21.64 | crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor |
| 3.4.21.64 | Langmuir-Blodgett nanotemplate method and hanging drop vapor diffusion method, using 400 mM Na/K-tartrate in 25 mM HEPES pH 7.0 |
| 3.4.21.64 | mercury-inhibited protein in presence of synthetic peptides GGGWGQPH and HGGGW, derived from N-terminal domain of human prion protein. Segment GGG is strongly bound as a substrate at the substrate recognition site |
| 3.4.21.64 | purified enzyme, oil microbatch method, mixing of 0.001 ml of 40 mg/ml protein solution in 50 mM MES-NaOH, pH 6.5, with 0.001 ml of precipitant solution composed of 250 mM NaNO3, 50 mM CaCl2, and 50 mM MES-NaOH, pH 6.5, to form Pr3+-derivatized crystals, the precipitant solution containing additionally 25 mM PrCl3 is used, X-ray diffraction structure determination and analysis at 1.45 A resolution |
| 3.4.21.64 | space group P4(3)2(1)2, cell dimensions a = b = 67.3 A, c = 106.6 A |
