title: Crystallization of the core protein of cellobiohydrolase II from Trichoderma reesei.
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.
authors: Department of Molecular Biology, Biomedical Centre, Uppsala, Sweden.
authors: T
authors: T
authors: Bergfors
authors: J
authors: J
authors: Rouvinen
authors: P
authors: P
authors: Lehtovaara
authors: X
authors: X
authors: Caldentey
authors: P
authors: P
authors: Tomme
authors: M
authors: M
authors: Claeyssens
authors: G
authors: G
authors: Pettersson
authors: T
authors: T
authors: Teeri
authors: J
authors: J
authors: Knowles
authors: T A
authors: TA
authors: Jones
mesh_terms: D043366:Cellulose 1,4-beta-Cellobiosidase; D003460:Crystallization; D005656:Fungal Proteins; D006026:Glycoside Hydrolases; D003904:Mitosporic Fungi; D011092:Polyethylene Glycols; D014242:Trichoderma; D014961:X-Ray Diffraction
chemical_list: D005656:Fungal Proteins; D011092:Polyethylene Glycols; D006026:Glycoside Hydrolases; D043366:Cellulose 1,4-beta-Cellobiosidase