Skip to main navigation Skip to search Skip to main content

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

  • SUNY Buffalo

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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.

Original languageEnglish
Pages (from-to)230-232
Number of pages3
JournalProteins: Structure, Function and Genetics
Volume11
Issue number3
DOIs
StatePublished - Nov 1991

Keywords

  • crystals
  • enzyme
  • parotid saliva
  • X‐ray analysis

Fingerprint

Dive into the research topics of 'Crystallization and preliminary X‐ray diffraction studies of human salivary α‐amylase'. Together they form a unique fingerprint.

Cite this