Journal article
Crystallization of barley malt alpha-amylases and preliminary x-ray diffraction studies of the high pI isozyme, alpha-amylase 2
In
Journal of Biological Chemistry
—
1987, Volume 262, Issue 28, pp. 13682-13684
Abstract
alpha-Amylase isozymes 1 and 2 isolated from germinated barley seeds have been crystallized by the hanging- or sitting-drop vapor diffusion technique. Crystals of alpha-amylase 2 suitable for x-ray diffraction analysis were grown at pH 6.7 and 22 degrees C from a solution of 1 mM calcium chloride, 10 mM MES, and 16% saturated ammonium sulfate.
The space group is trigonal P3121 (or P3221) with unit cell dimensions a = b = 135.20 A, c = 79.63 A, and probably two molecules per asymmetric unit.
| Language: | English |
|---|---|
| Year: | 1987 |
| Pages: | 13682-13684 |
| ISSN: | 1083351x and 00219258 |
| Types: | Journal article |
| DOI: | 10.1016/S0021-9258(19)76480-1 |
