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 language | English |
|---|---|
| Pages (from-to) | 230-232 |
| Number of pages | 3 |
| Journal | Proteins: Structure, Function and Genetics |
| Volume | 11 |
| Issue number | 3 |
| DOIs | |
| State | Published - 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
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver