Crystallization and preliminary X-ray study of porcine trypsin, free and complexed with Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family

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 Å. Crystals are orthorhombic, space group P2 12 12 1, with cell dimensions a = 77·32 A ̊ , b = 5...

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Veröffentlicht in:	Journal of molecular biology 1989-12, Vol.210 (4), p.883-884
Hauptverfasser:	Gaboriaud, C., Vaney, M.C., Bachet, B., Le-Nguyen, D., Castro, B., Mornon, J.P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Crystallography Ecballium elaterium Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases pigs Plant Proteins - ultrastructure Protein Conformation Swine Trypsin Trypsin Inhibitors - ultrastructure X-Ray Diffraction
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Beschreibung
Zusammenfassung:	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 Å. Crystals are orthorhombic, space group P2 12 12 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.
ISSN:	0022-2836 1089-8638
DOI:	10.1016/0022-2836(89)90118-6