期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 67, 期 -, 页码 1428-1431出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309111036244
关键词
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资金
- EPSRC [GR/R47950/01, GR/R99393/01, EP/C015452/1]
- EU [RII3-CT-2003-505925, NMP4-CT-2006-033256]
- Engineering and Physical Sciences Research Council [EP/C015452/1, GR/R47950/01] Funding Source: researchfish
- EPSRC [EP/C015452/1] Funding Source: UKRI
Preliminary studies of perdeuterated crystals of human transthyretin (TTR) have been carried out using the LADI-III and D19 diffractometers at the Institut Laue-Langevin in Grenoble. The results demonstrate the feasibility of a full crystallographic analysis to a resolution of 2.0 angstrom using Laue diffraction and also illustrate the potential of using monochromatic instruments such as D19 for higher resolution studies where larger crystals having smaller unit cells are available. This study will yield important information on hydrogen bonding, amino-acid protonation states and hydration in the protein. Such information will be of general interest for an understanding of the factors that stabilize/destabilize TTR and for the design of ligands that may be used to counter TTR amyloid fibrillogenesis.
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