title: Crystallization and preliminary X-ray diffraction studies of curculin. A new type of sweet protein having taste-modifying action.
abstract: A taste-modifying protein, curculin, has been crystallized by the vapor diffusion method using polyethylene glycol 400 as a precipitant. The crystals belong to orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions: a = 105 A, b = 271 A, c = 48.7 A. The crystals diffract X-rays to at least a resolution of 3.0 A and are suitable for X-ray crystallographic studies.
authors.affiliation: Department of Applied Chemistry, Faculty of Engineering Osaka University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Harada
authors.forename: H
authors.initials: H
authors.lastname: Otani
authors.forename: S
authors.initials: S
authors.lastname: Maeda
authors.forename: Y
authors.initials: Y
authors.lastname: Kai
authors.forename: N
authors.initials: N
authors.lastname: Kasai
authors.forename: Y
authors.initials: Y
authors.lastname: Kurihara
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D013649:Taste / Q000187:drug effects
chemical_list: D010940:Plant Proteins; C065630:curculin