A preliminary neutron crystallographic study of thaumatin.
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.
Teixeira
Susana C M
SC
ILL-EMBL Deuteration Laboratory, Partnership for Structural Biology, 6 Rue Jules Horowitz, 38042 Grenoble, France.
Blakeley
Matthew P
MP
Leal
Ricardo M F
RM
Mitchell
Edward P
EP
Forsyth
V Trevor
VT
D003460:Crystallization; D018360:Crystallography, X-Ray; D008956:Models, Chemical; D033363:Neutron Diffraction; D010940:Plant Proteins / Q000737:chemistry*
D010940:Plant Proteins; C003427:thaumatin protein, plant