Open AccessPurification, crystallization and preliminary crystallographic studies of a Kunitz‐type proteinase inhibitor from tamarind ( Tamarindus indica ) seeds
Author(s) -
Patil Dipak N.,
Chaudhry 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/s1744309109023495
Subject(s) - orthorhombic crystal system , crystallization , homogeneous , chemistry , proteinase inhibitor , crystallography , biochemistry , enzyme , crystal structure , organic chemistry , physics , thermodynamics
A Kunitz‐type proteinase inhibitor has been purified from tamarind ( Tamarindus indica ) seeds. SDS–PAGE analysis of a purified sample showed a homogeneous band corresponding to a molecular weight of 21 kDa. The protein was identified as a Kunitz‐type proteinase inhibitor based on N‐terminal amino‐acid sequence analysis. It was crystallized by the vapour‐diffusion method using PEG 6000. The crystals belonged to the orthorhombic space group C 222 1 , with unit‐cell parameters a = 37.2, b = 77.1, c = 129.1 Å. Diffraction data were collected to a resolution of 2.7 Å. Preliminary crystallographic analysis indicated the presence of one proteinase inhibitor molecule in the asymmetric unit, with a solvent content of 44%.