Preservatives prions

Cross-/] structure has been demonstrated for Sup35pNM filaments. Serio et al. (2000) observed a 0.47-nm reflection by X-ray diffraction, and subsequently this reflection was shown to be meridional both by X-ray fiber diffraction (Kishimoto et al., 2004) and electron diffraction (King and Diaz-Avalos, 2004). In the Ure2p system, cross-/ structure has been established by electron diffraction from prion domain filaments preserved in vitreous ice (Fig. 7 Baxa et al, 2005). In addition, a 0.47-nm reflection was detected by both X-ray diffraction and electron diffraction from filament preparations of full-length Ure2p and the Ure2p1 65-GFP fusion, indicating that they contain the same structure (Fig. 7 Baxa et al, 2005). 

In a third approach, Lindquist and her colleagues used fluorescent imaging and optical trapping techniques to analyze the forces which determine the integrity of yeast prion fibrils [56]. The results revealed strong non-covalent interactions that preserve the fibril structure even if individual fibrils unfold. 

Baron HS, Groth D, DeArmond SJ, Prusiner SB (2001) Prions. In Block SS (ed) Disinfection, sterilization and preservation. Lippincott, Philadelphia... 

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