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Title
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Crystallization of agglutinin from the seeds of Abrus precatorius.
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Authors
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K.Panneerselvam,
S.C.Lin,
C.L.Liu,
Y.C.Liaw,
J.Y.Lin,
T.H.Lu.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
898-899.
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PubMed id
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Abstract
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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%.
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