The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

REL 2020-08-19 2020-10-28 2020-10-28 The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure 0000-0002-4487-0230 David R. Boyer Department of Chemistry & Biochemistry, University of California, Los Angeles 611 Charles E. Young Drive East Los Angeles California United States 90095 0000-0002-4487-0230 David R. Boyer Department of Chemistry & Biochemistry, University of California, Los Angeles 611 Charles E. Young Drive East Los Angeles California United States 90095 Boyer DR Li B Sun C Fan W Zhou K Hughes MP Sawaya MR Jiang L Eisenberg DS 897.9 10.6019/EMPIAR-10494 EMDB EMD-20759 Boyer DR Li B Sun C Fan W Zhou K Hughes MP Sawaya MR Jiang L Eisenberg DS The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure Proceedings of the National Academy of Sciences of the United States of America Proc. Natl. Acad. Sci. U.S.A. United States 7 117 3592 3602 2020 English 10.1073/pnas.1917914117 32015135

Unaligned super-resolution K2 dose fractionated movies. 1.2 e/A^2/frame. Cs 2.7, 300 keV. Particle coordinates and gain file (no rotation/flipping necessary).

Unaligned K3 frames from alpha-synuclein E46K amyloid fibrils /data/movies micrographs - multiframe TIFF TIFF 4919 30 0 30 UNSIGNED BYTE 7676 0.422 7420 0.422

K2 super-resolution movies. 1.2 e/A^2/frame. 5 frame/second. Cs 2.7. 300 keV. Spot size 7. C2 Aperture 50 um. Gain does not need to be flipped. Coords are start/end only following eman2 helixboxer convention.

data/movies/*.tif data/coords/*boxes.txt data/coords