Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy

A strategy is described for solving the high-resolution structure of amyloid fibrils by solid-state NMR and is used for determining the atomic-resolution structure of the prion domain of the fungal prion HET-s in its amyloid form. A comprehensive protocol is described by using six differently labeled samples, a collection of optimized solid-state NMR experiments and adapted structure calculation protocols.