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Proteins. 1991;11(3):230-2.

Crystallization and preliminary X-ray diffraction studies of human salivary alpha-amylase.

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1
Department of Oral Biology, School of Dental Medicine, State University of New York, Buffalo 14214.

Abstract

Nonglycosylated alpha-amylase, a major component of human parotid saliva, has been crystallized by the vapor diffusion technique using 2-methyl-2,4-pentanediol as the precipitant in the presence of CaCl2 at pH 9.0. The crystals are orthorhombic, space group P2(1)2(1)2(1) with unit cell dimensions of a = 53.3, b = 75.8, and c = 138.1 A. The asymmetric unit contains one amylase molecule. The solvent content is 54%. The crystals are stable to X-rays and diffract up to 2.8 A and appear to be suitable for X-ray diffraction studies.

PMID:
1749776
DOI:
10.1002/prot.340110308
[Indexed for MEDLINE]
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