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Flow-aligned, single-shot fiber diffraction using a femtosecond X-ray free-electron laser.

Journal article
Authors David Popp
N Duane Loh
Habiba Zorgati
Umesh Ghoshdastider
Lu Ting Liow
Magdalena I Ivanova
Mårten Larsson
Daniel P DePonte
Richard Bean
Kenneth R Beyerlein
Cornelius Gati
Dominik Oberthuer
David Arnlund
Gisela Brändén
Peter Berntsen
Duilio Cascio
Leonard M G Chavas
Joe P J Chen
Ke Ding
Holger Fleckenstein
Lars Gumprecht
Rajiv Harimoorthy
Estelle Mossou
Michael R Sawaya
Aaron S Brewster
Johan Hattne
Nicholas K Sauter
Marvin Seibert
Carolin Seuring
Francesco Stellato
Thomas Tilp
David S Eisenberg
Marc Messerschmidt
Garth J Williams
Jason E Koglin
Lee Makowski
Rick P Millane
Trevor Forsyth
Sébastien Boutet
Thomas A White
Anton Barty
Henry Chapman
Swaine L Chen
Mengning Liang
Richard Neutze
Robert C Robinson
Published in Cytoskeleton (Hoboken, N.J.)
Volume 74
Issue 12
Pages 472-481
ISSN 1949-3592
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Pages 472-481
Language en
Links dx.doi.org/10.1002/cm.21378
www.ncbi.nlm.nih.gov/entrez/query.f...
https://gup.ub.gu.se/file/207140
Subject categories Structural Biology

Abstract

A major goal for X-ray free-electron laser (XFEL) based science is to elucidate structures of biological molecules without the need for crystals. Filament systems may provide some of the first single macromolecular structures elucidated by XFEL radiation, since they contain one-dimensional translational symmetry and thereby occupy the diffraction intensity region between the extremes of crystals and single molecules. Here, we demonstrate flow alignment of as few as 100 filaments (Escherichia coli pili, F-actin, and amyloid fibrils), which when intersected by femtosecond X-ray pulses result in diffraction patterns similar to those obtained from classical fiber diffraction studies. We also determine that F-actin can be flow-aligned to a disorientation of approximately 5 degrees. Using this XFEL-based technique, we determine that gelsolin amyloids are comprised of stacked β-strands running perpendicular to the filament axis, and that a range of order from fibrillar to crystalline is discernable for individual α-synuclein amyloids.

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