title: Crystallization and preliminary X-ray study of porcine trypsin, free and complexed with Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family.
abstract: Porcine trypsin has been crystallized either free or complexed with synthetic Ecballium elaterium trypsin inhibitor II, a 28-residue peptide with three disulfide bridges. The crystals diffract beyond 2.0 A. Crystals are orthorhombic, space group P2(1)2(1)2(1), with cell dimensions a = 77.32 A, b = 53.81 A, c = 46.91 A, for the free trypsin, and a = 62.25 A, b = 62.27 A, c = 84.66 A for the complex with E. elaterium trypsin inhibitor II.
authors.affiliation: Laboratoire de Minéralogie-Cristallographie, CNRS URA09, Université P6, Paris, France.
authors.forename: C
authors.initials: C
authors.lastname: Gaboriaud
authors.forename: M C
authors.initials: MC
authors.lastname: Vaney
authors.forename: B
authors.initials: B
authors.lastname: Bachet
authors.forename: D
authors.initials: D
authors.lastname: Le-Nguyen
authors.forename: B
authors.initials: B
authors.lastname: Castro
authors.forename: J P
authors.initials: JP
authors.lastname: Mornon
mesh_terms: D000818:Animals; D003461:Crystallography; D010940:Plant Proteins / Q000648:ultrastructure; D011487:Protein Conformation; D013552:Swine; D014357:Trypsin; D014361:Trypsin Inhibitors / Q000648:ultrastructure*; D014961:X-Ray Diffraction
chemical_list: D010940:Plant Proteins; D014361:Trypsin Inhibitors; D014357:Trypsin