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Updated: Aug 10, 2026

Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
Crystallization and preliminary X-ray characterization of a lectin from Cicer arietinum (chickpea)
Uma V Katre1, S M Gaikwad, S S Bhagyawant
1Division of Biochemical Sciences, National Chemical Laboratory, Pune 411008, India.
Abstract:
The lectin isolated from mature seeds of Cicer arietinum (CAL) agglutinates pronase-treated rabbit and human erythrocytes and its haemagglutination activity is inhibited by fetuin and desialated fetuin but not by simple monosaccharides or oligosaccharides. The purified lectin is a dimer of molecular weight 43,000 Da composed of two identical subunits (MW 21,500), as confirmed by SDS-PAGE. The lectin has been crystallized using the hanging-drop vapour-diffusion method at 295 K over a well solution containing 0.2 M sodium acetate, 0.1 M sodium phosphate buffer pH 6.5 and 14%(w/v) polyethylene glycol 8000. The triangular prism-shaped crystals belong to space group R3 and have unit-cell parameters a = b = 81.2, c = 69.4 A. The diffraction data are 93.8% complete to 2.3 A Bragg spacing with an Rmerge of 0.103.

