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TitleFibril structure of amyloid-β(1-42) by cryo-electron microscopy.
Journal, issue, pagesScience, Vol. 358, Issue 6359, Page 116-119, Year 2017
Publish dateOct 6, 2017
AuthorsLothar Gremer / Daniel Schölzel / Carla Schenk / Elke Reinartz / Jörg Labahn / Raimond B G Ravelli / Markus Tusche / Carmen Lopez-Iglesias / Wolfgang Hoyer / Henrike Heise / Dieter Willbold / Gunnar F Schröder
External linksPubMed:28882996 / Publisher's page
KeywordsAmyloid beta-Peptides / Cryoelectron Microscopy / Humans / Nuclear Magnetic Resonance, Biomolecular / Peptide Fragments / Protein Multimerization / Protein Structure, Secondary / X-Ray Diffraction / amyloid beta-protein (1-42) / PROTEIN FIBRIL / amyloid / fibril / aggregation / Alzheimer's disease / Protein fibril
MethodsEM (helical sym.)
Resolution4 A
Structure data

EMDB-3851:
Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM

PDB-5oqv:
Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM

Source
  • Homo sapiens (human)
  • homo sapiens (human)

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