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Crystallization and preliminary X-ray diffraction studies of curculin. A new type of sweet protein having
1Department of Applied Chemistry, Faculty of Engineering Osaka University, Japan.
Journal of Molecular Biology
|April 29, 1994
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.