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Literature summary for 3.4.21.4 extracted from

  • Liebschner, D.; Dauter, M.; Brzuszkiewicz, A.; Dauter, Z.
    On the reproducibility of protein crystal structures: five atomic resolution structures of trypsin (2013), Acta Crystallogr. Sect. D, 69, 1447-1462.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis 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 Bos taurus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00760
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