Crystallization of the core protein of cellobiohydrolase II from Trichoderma reesei.
作者信息
Bergfors T, Rouvinen J, Lehtovaara P, Caldentey X, Tomme P, Claeyssens M, Pettersson G, Teeri T, Knowles J, Jones T A
机构信息
Department of Molecular Biology, Biomedical Centre, Uppsala, Sweden.
出版信息
J Mol Biol. 1989 Sep 5;209(1):167-9. doi: 10.1016/0022-2836(89)90179-4.
PMID:2810367
Abstract
Single crystals of the core protein of the cellulase cellobiohydrolase II have been grown in polyethylene glycol 6000 with the hanging drop method. Successful crystallization occurred only when 82 amino acids were removed from the N terminus by papain cleavage. Crystals belong to the space group P2(1) and have cell constants a = 49.1 A, b = 75.8 A, c = 92.9 A, beta = 103.2. The diffraction pattern extends to better than 2.0 A.
摘要
Zotero 插件