Crystallization and preliminary X-ray characterization of a lectin from Cicer arietinum (chickpea).
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.
Katre
Uma V
UV
Division of Biochemical Sciences, National Chemical Laboratory, Pune 411008, India.
Gaikwad
S M
SM
Bhagyawant
S S
SS
Deshpande
U D
UD
Khan
M I
MI
Suresh
C G
CG
D000595:Amino Acid Sequence; D029863:Cicer / Q000737:chemistry*; D002942:Circular Dichroism; D017124:Conserved Sequence; D003460:Crystallization; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D037121:Plant Lectins; D021122:Protein Subunits