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

Authors

  • Dr. Narayanan Ramasubbu,

    Corresponding author
    1. Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, New York 14214
    • Department of Oral Biology, Foster Hall, School of Dental Medicine, State University of New York, Buffalo, NY 14214-3092
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  • Krishna K. Bhandary,

    1. Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, New York 14214
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  • Frank A. Scannapieco,

    1. Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, New York 14214
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  • Michael J. Levine

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

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