EC Number   |
|---|
   3.4.21.97 | - |
| 3.4.21.97 | crystal structure at 2.0 A resolution |
| 3.4.21.97 | crystal structure at 2.27 A resolution |
| 3.4.21.97 | crystal structure of HAS-2 with covalently bound diisopropyl fluorophosphate |
| 3.4.21.97 | crystal structure of HCMV protease in complex with the peptidomimetic inhibitor BILC 821 as protease model. Only the dimeric form of the protease is able to reorient the main-chain atoms of Arg165 along the reaction coordinate in order to stabilize more efficiently the oxyanion formed in the reaction pathway |
| 3.4.21.97 | crystal structure of the catalytic domain at 2.5 A resolution |
| 3.4.21.97 | hanging drop method, microseeding technique, each of six components in the final crystallization formula (16% polyethylene glycol 4000, 0.1 M MES pH 6.0, 0.4 M LiCl, 10% glycerol 5% tert-butanol and 5 mM Na2S2O3) plays a distinctive role and is indispensable. Free enzyme crystallizes at pH 6.0. Using 20-50 mM spermine in the crystallization buffer, crystals of two peptidomimetic inhibitor complexes with C821 are obtained at pH 7.5 and pH 8.0. Spermine is required for the inhibitor complexes to be crystallized at pH 8.0, possibly neutralizing net negative charges of the enzyme owing to its acidic pI of 5.5 |
| 3.4.21.97 | hanging drop vapour diffusion method, wild-type and mutant enzymes |
| 3.4.21.97 | hanging-drop vapor diffusion method, crystal structure of the wild-typelike mutant enzyme A143Q in complex with peptidomimetic inhibitors, crystal structure of peptidomimetic inhibitor in complex with the E31R mutant enzyme |
| 3.4.21.97 | in complex with inhibitors 3_4_21-97_3-cp2 and 3_4_21-97_3-cp3 |
