The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy

Acta Crystallographica Section D: Biological Crystallography

Volumn 71, Issue , 2015, Pages 882-895

  Langkilde, Annette E ^a   Morris, Kyle L ^b   Serpell, Louise C ^b   Svergun, Dmitri I ^c   Vestergaard, Bente ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

amyloid like fibril; electron microscopy; fibre diffraction; fibril structure; hierarchical assembly; hybrid structural analysis; small angle X ray scattering

Indexed keywords

AMYLOID; PRION; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; TRANSLATION TERMINATION FACTOR;

AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON MICROSCOPY; PRION; PROTEIN SECONDARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SMALL ANGLE SCATTERING; ULTRASTRUCTURE; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; AMYLOID; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; PEPTIDE TERMINATION FACTORS; PRIONS; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SCATTERING, SMALL ANGLE; X-RAY DIFFRACTION;

EID: 84927653764     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004715001674     Document Type: Article

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