Crystallization and preliminary X-ray diffraction analysis of the complex of Kunitz-type tamarind trypsin inhibitor and porcine pancreatic trypsin.
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%.
Tomar
Sakshi
S
Department of Biotechnology, Indian Institute of Technology, Roorkee, India.
Patil
Dipak N
DN
Datta
Manali
M
Tapas
Satya
S
Preeti
Chaudhary
Anshul
A
Sharma
Ashwani K
AK
Tomar
Shailly
S
Kumar
Pravindra
P
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
C053865:Kunitz-type protease inhibitor, plant; D010455:Peptides; D010940:Plant Proteins; D014357:Trypsin