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J. Biochem, 1994, Vol. 115, No. 2 179-181
© 1994 Japanese Biochemical Society

other

Crystallization and Preliminary X-Ray Diffraction Studies of the {alpha}-Amylase Inhibitor Coded 0.19 from Wheat Kernel1

Toshiyuki Miyazaki*, Toshibisa Morimoto*, Keiichi Fukuyama**,2 and Hiroshi Matsubara**

*Cereal Food R&D Section, Food Research Laboratory, Nisshin Flour Milling Co, Ltd. Iruma, Saitama 356
**Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560

2To whom correspondence should be addressed.

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 P31 or P32, 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.

1This research was supported in part by a Grant-in-Aid for Cooperative Research (No. 03303014) to KF from the Ministry of Education, Science and Culture of Japan.


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