A preliminary neutron crystallographic study of thaumatin
- ILL-EMBL Deuteration Laboratory, Partnership for Structural Biology, 6 Rue Jules Horowitz, 38042 Grenoble (France)
- Institut Laue Langevin, 6 Rue Jules Horowitz, 38042 Grenoble (France)
- EPSAM and ISTM, Keele University, Staffordshire ST5 5BG (United Kingdom)
Preliminary neutron crystallographic data from the sweet protein thaumatin have been recorded using the LADI-III diffractometer at the Institut Laue Langevin (ILL). The results illustrate the feasibility of a full neutron structural analysis aimed at further understanding the molecular basis of the perception of sweet taste. Such an analysis will exploit the use of perdeuterated 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 Å 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.
- OSTI ID:
- 22360568
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 5; Other Information: PMCID: PMC2376403; PMID: 18453706; PUBLISHER-ID: fw5174; OAI: oai:pubmedcentral.nih.gov:2376403; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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