Crystallographic study of endogenous α-amylase inhibitor from wheat

Autor: Koji Maeda, Mamoru Sato, Yasuo Hata, Yukiteru Katsube, Hiroshi Matsubara, Youichi Kato, Nobuo Tanaka
Rok vydání: 1987
Předmět:
Zdroj: Journal of Molecular Biology. 193:825-826
ISSN: 0022-2836
DOI: 10.1016/0022-2836(87)90364-0
Popis: Endogenous α-amylase inhibitor from wheat has been crystallized by a microdialysis method. There are two forms of monoclinic crystal in a microdialysis cell with a space group of P 2 1 . The unit cell dimensions are a = 43.5 A , b = 64.8 A , c = 32.2 A , β = 113 ° for the rod-like crystal, and a = 42.5 A , b = 65.2 A , c = 32.2 A , β = 112 ° for the plate-like crystal. The former is suitable for structure analysis because it gives the sharp diffraction beyond 2.0 A resolution, and the latter tends to form a twin crystal. A heavy-atom derivative has been successfully prepared with the heavy-atom reagent K 2 PtCl 4 , and structure analysis is in progress.
Databáze: OpenAIRE