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Crystallization and preliminary X-ray diffraction studies of the alpha-amylase inhibitor coded 0.19 from wheat kernel.

作者信息

Miyazaki T, Morimoto T, Fukuyama K, Matsubara H

机构信息

Cereal Food R&D Section, Nisshin Flour Milling Co., Ltd., Saitama.

出版信息

J Biochem. 1994 Feb;115(2):179-81. doi: 10.1093/oxfordjournals.jbchem.a124314.

DOI:10.1093/oxfordjournals.jbchem.a124314
PMID:8206864
Abstract

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.

摘要

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