Correlation of structural elements and infectivity of the HET-s prion

Alzheimer's, prion diseases and other neurodegenerative disorders are associated with insoluble protein fibres called amyloid fibrils. Gathering structural information about these has proved difficult, but three groups now report success with contrasting approaches to the problem. The cover shows the atomic structure of the ‘spine’ of an amyloid-like fibril formed by the yeast prion protein Sup35. To obtain this structure, Nelson et al. performed X-ray crystallography on amyloid microcrystals. Krishnan and Lindquist used a raft of techniques to study folding of the amyloid core. And Ritter et al. determined the infectious conformation of HET-s prion of a filamentous fungus. Christopher Dobson ponders on what this flood of structural data says about prion and amyloid formation in sickness and in health.