Fig. 3
From: Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
Secondary structure comparison of the PI3K-SH3 DF fibril. Secondary structure of the presented cryo-EM structure compared to data obtained previously by solid-state NMR (fibrils) or liquid-state NMR (monomeric, native state). a Tilted cross-section of four SH3 DF fibril layers. Secondary structure is predominantly formed by seven cross-β sheets. b Secondary structure comparison to the native solution structure (PDB: 1PKS28) and ssNMR results (fibrils) modified according to Bayro et al.38. Flexible regions are shown as dashed lines, β-sheets as arrows, and the helix as a cylinder
