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Title
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Purification and crystallization of Shiga toxin from Shigella dysenteriae.
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Authors
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Y.V.Kozlov,
M.M.Chernaia,
M.E.Fraser,
M.N.James.
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Ref.
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J Mol Biol, 1993,
232,
704-706.
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PubMed id
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Abstract
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The protein toxin produced by Shigella dysenteriae consists of one enzymatically
active A subunit of 293 amino acid residues and five B subunits of 69 amino acid
residues that are involved with cell attachment. The holotoxin has been purified
by blue Sepharose and chromatofocusing column chromatography. Two crystal forms
of purified holotoxin have been grown by vapor diffusion. One grows as fine
needles, hexagonal in cross-section, which do not diffract well enough to
characterize crystallographically. The second grows as thin plates that diffract
to at least 3 A resolution. Their space group is P2(1)2(1)2(1) with unit cell
dimensions of a = 132.0 A, b = 146.0 A and c = 82.5 A. The asymmetric unit of
the crystals is likely to contain two AB5 units.
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