Crystallization and preliminary X‐ray diffraction studies of human salivary α‐amylase
- 1 November 1991
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 11 (3) , 230-232
- https://doi.org/10.1002/prot.340110308
Abstract
Nonglycosylated α-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 P212121 with unit cell dimensions of a = 53.3, b = 75.8, and c = 138.1 Å. 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 Å and appear to be suitable for X-ray diffraction studies.Keywords
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