title: Crystallization and preliminary X-ray diffraction analysis of the complex of Kunitz-type tamarind trypsin inhibitor and porcine pancreatic trypsin.
abstract: The complex of Tamarindus indica Kunitz-type trypsin inhibitor and porcine trypsin has been crystallized by the sitting-drop vapour-diffusion method using ammonium acetate as precipitant and sodium acetate as buffer. The homogeneity of complex formation was checked by size-exclusion chromatography and further confirmed by reducing SDS-PAGE. The crystals diffracted to 2.0 angstrom resolution and belonged to the tetragonal space group P4(1), with unit-cell parameters a = b = 57.1, c = 120.1 angstrom. Preliminary X-ray diffraction analysis indicated the presence of one unit of inhibitor-trypsin complex per asymmetric unit, with a solvent content of 45%.
authors.affiliation: Department of Biotechnology, Indian Institute of Technology, Roorkee, India.
authors.forename: Sakshi
authors.initials: S
authors.lastname: Tomar
authors.forename: Dipak N
authors.initials: DN
authors.lastname: Patil
authors.forename: Manali
authors.initials: M
authors.lastname: Datta
authors.forename: Satya
authors.initials: S
authors.lastname: Tapas
authors.lastname: Preeti
authors.forename: Anshul
authors.initials: A
authors.lastname: Chaudhary
authors.forename: Ashwani K
authors.initials: AK
authors.lastname: Sharma
authors.forename: Shailly
authors.initials: S
authors.lastname: Tomar
authors.forename: Pravindra
authors.initials: P
authors.lastname: Kumar
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry; D034421:Sus scrofa; D029861:Tamarindus / Q000033:anatomy & histology / Q000737:chemistry*; D014357:Trypsin / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: C053865:Kunitz-type protease inhibitor, plant; D010455:Peptides; D010940:Plant Proteins; D014357:Trypsin