Open AccessCrystallization and preliminary X‐ray diffraction analysis of the complex of Kunitz‐type tamarind trypsin inhibitor and porcine pancreatic trypsin
Author(s) -
Tomar Sakshi,
Patil Dipak N.,
Datta Manali,
Tapas Satya,
Chaudhary Anshul,
Sharma Ashwani K.,
Tomar Shailly,
Kumar Pravindra
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109041694
Subject(s) - trypsin , crystallization , trypsin inhibitor , x ray , chemistry , crystallography , x ray crystallography , diffraction , materials science , biochemistry , enzyme , organic chemistry , physics , optics
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 Å resolution and belonged to the tetragonal space group P 4 1 , with unit‐cell parameters a = b = 57.1, c = 120.1 Å. Preliminary X‐ray diffraction analysis indicated the presence of one unit of inhibitor–trypsin complex per asymmetric unit, with a solvent content of 45%.