Crystallization of agglutinin from the seeds of Abrus precatorius.
Agglutinin protein purified from the seeds of Abrus precatorius has a high antitumour activity and was crystallized at room temperature with polyethylene glycol 8000 as the precipitant. The agglutinin crystal diffracted to 3.45 A and belongs to one of two possible tetragonal space groups, P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 141.91, c = 105.63 A. The asymmetric unit contains a heterotetrameric protein molecule of molecular weight 134 kDa and has a solvent content of approximately 38%.
Department of Physics, National Tsing Hua University, Hsinchu 30055, Taiwan.
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Panneerselvam
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Lin
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Liu
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Liaw
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JY
Lin
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Lu
D003460:Crystallization; D018360:Crystallography, X-Ray; D037102:Lectins / Q000737:chemistry*; D037121:Plant Lectins; D011487:Protein Conformation; D014407:Tumor Cells, Cultured
D037102:Lectins; D037121:Plant Lectins; C016940:abrus agglutinin