Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Guerrero-Ferreira, Ricardo; M. I. Taylor, Nicholas; Arteni, Ana‐Andreea; Kumari, Pratibha; Mona, Daniel; Ringler, Philippe; Britschgi, Markus; E. Lauer, Matthias; Makky, Ali; Verasdonck, Joeri; Riek, Roland; Melki, Ronald; H. Meier, Beat; Böckmann, Anja; Bousset, Luc; Stahlberg, Henning

doi:10.7554/elife.48907

Public

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Published in eLife • Dec 9, 2019

Authors:

Ricardo Guerrero-Ferreira

Nicholas M. I. Taylor

Ana‐Andreea Arteni

Abstract

Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson's disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1-121), composed of two protofibrils that are connected via a densely-packed interface ...

Subject

Fibril

Alpha-synuclein

Crystallography

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