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Title
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Crystallization and preliminary X-ray diffraction studies of the alpha-amylase inhibitor coded 0.19 from wheat kernel.
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Authors
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T.Miyazaki,
T.Morimoto,
K.Fukuyama,
H.Matsubara.
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Ref.
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J Biochem (tokyo), 1994,
115,
179-181.
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PubMed id
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Abstract
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The alpha-amylase inhibitor coded 0.19 (0.19AI) from wheat kernel is a dimeric
protein which inactivates exogenous alpha-amylases. Crystals of 0.19AI were
grown at room temperature and pH 7.0 from a protein solution with a low salt
concentration. They were trigonal, belonged to space group P3(1) or P3(2), and
had unit cell dimensions of a = b = 79.3 A and c = 60.8 A. The crystals diffract
X-rays to at least 2.0 A resolution and are stable to X-ray beams. The
asymmetric unit appears to contain two 0.19AI dimers. A potential heavy-atom
derivative was prepared by soaking the crystal in a HgCl2 solution.
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