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Cryo electron microscopy of ex-vivo human SAA amyloid fibrils

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SUBMITTER: Matthias Schmidt 

PROVIDER: EMPIAR-10734 | biostudies-other |

REPOSITORIES: biostudies-other

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Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.

Liberta Falk F   Loerch Sarah S   Rennegarbe Matthies M   Schierhorn Angelika A   Westermark Per P   Westermark Gunilla T GT   Hazenberg Bouke P C BPC   Grigorieff Nikolaus N   Fändrich Marcus M   Schmidt Matthias M  

Nature communications 20190307 1

Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, we report the purification and electron cryo-microscopy analysis of amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The obtained resolutions are 3.0 Å and 2.7 Å for the murine and human fibril, respectively. The two fibrils differ in fundamental properties, such as pres  ...[more]

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