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Title
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Crystallization and a preliminary X-ray crystallographic study of alpha-amylase from Bacillus licheniformis.
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Authors
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S.Y.Lee,
S.Kim,
R.M.Sweet,
S.W.Suh.
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Ref.
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Arch Biochem Biophys, 1991,
291,
255-257.
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PubMed id
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Abstract
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alpha-Amylase from Bacillus licheniformis has been crystallized by the
hanging-drop vapor diffusion method in the presence of calcium ions using
ammonium sulfate as precipitant. The crystals are tetragonal, belonging to the
space group P4(1)2(1)2 (or P4(3)2(1)2), with unit cell dimensions of a = 119.9
and c = 85.4 A. The asymmetric unit contains one molecule of alpha-amylase, with
a crystal volume per protein mass (VM) of 2.78 A3/Da. The crystals diffract to
better than 2.0 A Bragg spacing when exposed to synchrotron X-rays and they are
reasonably stable in the X-ray beam. Thus the crystals are suitable for
structure determination at high resolution by X-ray methods.
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