EC Number   |
|---|
   3.4.21.4 | - |
| 3.4.21.4 | a series of crystal structures of trypsin, containing either an autoproteolytic cleaved peptide fragment or a covalently bound inhibitor. Cocrystallization with PMSF or DFP |
| 3.4.21.4 | analysis of membrane crystallization technique of benzamidine inhibited enzyme. Study on parameters to gain high control on the final properties of the crystalline material |
| 3.4.21.4 | analysis of structures at three different pH-values and two different temperatures, comparison with more trypsin structures |
| 3.4.21.4 | batch crystallization method, with 4 mM CaCl2, 90 mM benzamidine and 2.1 M ammonium sulfate |
| 3.4.21.4 | comparison of five crystals of bovine trypsin obtained under analogous conditions. The Calpha and backbone atoms of the structures superpose very well. The occupancy of ligands in regions of low thermal motion is reproducible, whereas solvent molecules containing heavier atoms (such as sulfur) or those located on the surface can differ significantly. The coordination lengths of the calcium ion are conserved. A large proportion of the multiple conformations refine to similar occupancies and the residues adopt similar orientations. The protonation states of histidine residues and carboxylate moieties is consistent for all of the models. However, several features of residues or ligands located in flexible parts of the macromolecule may vary significantly, such as side-chain orientations and the occupancies of certain fragments |
| 3.4.21.4 | crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 A resolution |
| 3.4.21.4 | crystal structure of epsilon-trypsin |
| 3.4.21.4 | crystal structure of the enzyme-benzylamine complex, enzyme-phenylethylamine complex and the enzyme-phenylbutylamine complex |
| 3.4.21.4 | crystal structure of the enzyme-benzylamine complex, enzyme-phenylethylamine complex and the enzyme-phenylpropylamine complex |
