Femtosecond X-ray coherent diffraction of aligned amyloid fibrils on low background graphene

DOI: 10.1038/s41467-018-04116-9

Authors: Carolin Seuring (Deutsches Elektronen-Synchrotron) , Kartik Ayyer (Deutsches Elektronen-Synchrotron) , Eleftheria Filippaki (Deutsches Elektronen-Synchrotron) , Miriam Barthelmess (Deutsches Elektronen-Synchrotron) , Jean-Nicolas Longchamp (Deutsches Elektronen-Synchrotron) , Philippe Ringler (University of Basel) , Tommaso Pardini (Lawrence Livermore National Laboratory) , David H. Wojtas (University of Canterbury) , Matthew A. Coleman (Lawrence Livermore National Laboratory) , Katerina Dörner (Deutsches Elektronen-Synchrotron) , Silje Fuglerud (Deutsches Elektronen-Synchrotron) , Greger Hammarin (University of Gothenburg) , Birgit Habenstein (CNRS, Université de Bordeaux) , Annette E. Langkilde (University of Copenhagen) , Antoine Loquet (CNRS, Université de Bordeaux) , Alke Meents (Deutsches Elektronen-Synchrotron) , Roland Riek (ETH Zürich) , Henning Stahlberg (University of Basel) , Sébastien Boutet (Linac Coherent Light Source) , Mark S. Hunter (Linac Coherent Light Source) , Jason Koglin (Linac Coherent Light Source) , Mengning Liang (Linac Coherent Light Source) , Helen M. Ginn (The Wellcome Trust Centre for Human Genetics, University of Oxford; Diamond Light Source) , Rick P. Millane (University of Canterbury) , Matthias Frank (Lawrence Livermore National Laboratory) , Anton Barty (Deutsches Elektronen-Synchrotron) , Henry N. Chapman (Deutsches Elektronen-Synchrotron; The Hamburg Centre for Ultrafast Imaging; University of Hamburg)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 9

State: Published (Approved)
Published: May 2018

Abstract: Here we present a new approach to diffraction imaging of amyloid fibrils, combining a free-standing graphene support and single nanofocused X-ray pulses of femtosecond duration from an X-ray free-electron laser. Due to the very low background scattering from the graphene support and mutual alignment of filaments, diffraction from tobacco mosaic virus (TMV) filaments and amyloid protofibrils is obtained to 2.7 Å and 2.4 Å resolution in single diffraction patterns, respectively. Some TMV diffraction patterns exhibit asymmetry that indicates the presence of a limited number of axial rotations in the XFEL focus. Signal-to-noise levels from individual diffraction patterns are enhanced using computational alignment and merging, giving patterns that are superior to those obtainable from synchrotron radiation sources. We anticipate that our approach will be a starting point for further investigations into unsolved structures of filaments and other weakly scattering objects.

Journal Keywords: Biological physics; Imaging techniques; Peptide hormones; Protein aggregation; Structural biology

Subject Areas: Technique Development, Biology and Bio-materials, Physics

Facility: DESY (XFEL)

Added On: 22/05/2018 16:01

Documents:
s41467-018-04116-9.pdf

Discipline Tags:

Neurodegenerative Diseases Non-Communicable Diseases Health & Wellbeing Technique Development - Life Sciences & Biotech Neurology Biophysics Life Sciences & Biotech

Technical Tags: