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

✍ Scribed by Dr. Narayanan Ramasubbu; Krishna K. Bhandary; Frank A. Scannapieco; Michael J. Levine

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
338 KB
Volume
11
Category
Article
ISSN
0887-3585

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✦ Synopsis

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 CaCl~2~ at pH 9.0. The crystals are orthorhombic, space group __P__2~1~2~1~2~1~ 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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