Analysis of XFEL serial diffraction data from individual crystalline fibrils

Author:

Wojtas David H.,Ayyer Kartik,Liang Mengning,Mossou Estelle,Romoli Filippo,Seuring Carolin,Beyerlein Kenneth R.,Bean Richard J.,Morgan Andrew J.,Oberthuer Dominik,Fleckenstein Holger,Heymann Michael,Gati Cornelius,Yefanov Oleksandr,Barthelmess Miriam,Ornithopoulou Eirini,Galli Lorenzo,Xavier P. Lourdu,Ling Wai Li,Frank Matthias,Yoon Chun Hong,White Thomas A.,Bajt Saša,Mitraki Anna,Boutet Sebastien,Aquila Andrew,Barty Anton,Forsyth V. Trevor,Chapman Henry N.,Millane Rick P.

Abstract

Serial diffraction data collected at the Linac Coherent Light Source from crystalline amyloid fibrils delivered in a liquid jet show that the fibrils are well oriented in the jet. At low fibril concentrations, diffraction patterns are recorded from single fibrils; these patterns are weak and contain only a few reflections. Methods are developed for determining the orientation of patterns in reciprocal space and merging them in three dimensions. This allows the individual structure amplitudes to be calculated, thus overcoming the limitations of orientation and cylindrical averaging in conventional fibre diffraction analysis. The advantages of this technique should allow structural studies of fibrous systems in biology that are inaccessible using existing techniques.

Funder

Helmholtz-Gemeinschaft

U.S. Department of Energy, Lawrence Livermore National Laboratory

National Institutes of Health

Fondation pour la Recherche Médicale

Centre National de la Recherche Scientifique

U.S. Department of Energy, Basic Energy Sciences

Publisher

International Union of Crystallography (IUCr)

Subject

Condensed Matter Physics,General Materials Science,Biochemistry,General Chemistry

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