title: A preliminary neutron crystallographic study of thaumatin.
abstract: A preliminary neutron crystallographic study of the sweet protein thaumatin is presented. Large hydrogenated crystals were prepared in deuterated crystallization buffer using the gel-acupuncture method. Data were collected to a resolution of 2 A on the LADI-III diffractometer at the Institut Laue Langevin (ILL). The results demonstrate the feasibility of a full neutron crystallographic analysis of this structure aimed at providing relevant information on the location of H atoms, the distribution of charge on the protein surface and localized water in the structure. This information will be of interest for understanding the specificity of thaumatin-receptor interactions and will contribute to further understanding of the molecular mechanisms underlying the perception of taste.
authors.affiliation: ILL-EMBL Deuteration Laboratory, Partnership for Structural Biology, 6 Rue Jules Horowitz, 38042 Grenoble, France.
authors.forename: Susana C M
authors.initials: SC
authors.lastname: Teixeira
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Blakeley
authors.forename: Ricardo M F
authors.initials: RM
authors.lastname: Leal
authors.forename: Edward P
authors.initials: EP
authors.lastname: Mitchell
authors.forename: V Trevor
authors.initials: VT
authors.lastname: Forsyth
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D008956:Models, Chemical; D033363:Neutron Diffraction; D010940:Plant Proteins / Q000737:chemistry*
chemical_list: D010940:Plant Proteins; C003427:thaumatin protein, plant