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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%.[1]

References

  1. Crystallization of agglutinin from the seeds of Abrus precatorius. Panneerselvam, K., Lin, S.C., Liu, C.L., Liaw, Y.C., Lin, J.Y., Lu, T.H. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
 
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