Structure of the toxic core of α-synuclein from invisible crystals

Rodriguez, Jose A.; Ivanova, Magdalena I.; Sawaya, Michael R.; Cascio, Duilio; Reyes, Francis E.; Shi, Dan; Sangwan, Smriti; Guenther, Elizabeth L.; Johnson, Lisa M.; Zhang, Meng; Jiang, Lin; Arbing, Mark A.; Nannenga, Brent L.; Hattne, Johan; Whitelegge, Julian; Brewster, Aaron S.; Messerschmidt, Marc; Boutet, Sébastien; Sauter, Nicholas K.; Gonen, Tamir; Eisenberg, David S.

doi:10.1038/nature15368

Title: Structure of the toxic core of α-synuclein from invisible crystals

Journal Article · Wed Sep 09 00:00:00 EDT 2015 · Nature (London)

DOI:https://doi.org/10.1038/nature15368· OSTI ID:1222837

Rodriguez, Jose A. ^[1]; Ivanova, Magdalena I. ^[1]; Sawaya, Michael R. ^[1]; Cascio, Duilio ^[1]; Reyes, Francis E. ^[2]; Shi, Dan ^[2]; Sangwan, Smriti ^[1]; Guenther, Elizabeth L. ^[1]; Johnson, Lisa M. ^[1]; Zhang, Meng ^[1]; Jiang, Lin ^[1]; Arbing, Mark A. ^[1]; Nannenga, Brent L. ^[2]; Hattne, Johan ^[2]; Whitelegge, Julian ^[3]; Brewster, Aaron S. ^[4]; Messerschmidt, Marc ^[5]; Boutet, Sébastien ^[5]; Sauter, Nicholas K. ^[4]; Gonen, Tamir ^[2] more »

Univ. of California, Los Angeles, CA (United States). Howard Hughes Medical Institute/UCLA-DOE Institute
Howard Hughes Medical Institute, Ashburn, VA (United States)
Univ. of California, Los Angeles, CA (United States). NPI-Semel Institute
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
SLAC National Accelerator Lab., Menlo Park, CA (United States). Linac Coherent Light Source (LCLS)

The protein α-synuclein is the main component of Lewy bodies, the neuron-associated aggregates seen in Parkinson disease and other neurodegenerative pathologies. An 11-residue segment, which we term NACore, appears to be responsible for amyloid formation and cytotoxicity of human α-synuclein. Here we describe crystals of NACore that have dimensions smaller than the wavelength of visible light and thus are invisible by optical microscopy. As the crystals are thousands of times too small for structure determination by synchrotron X-ray diffraction, we use micro-electron diffraction to determine the structure at atomic resolution. The 1.4 Å resolution structure demonstrates that this method can determine previously unknown protein structures and here yields, to our knowledge, the highest resolution achieved by any cryo-electron microscopy method to date. The structure exhibits protofibrils built of pairs of face-to-face β-sheets. X-ray fibre diffraction patterns show the similarity of NACore to toxic fibrils of full-length α-synuclein. The NACore structure, together with that of a second segment, inspires a model for most of the ordered portion of the toxic, full-length α-synuclein fibril, presenting opportunities for the design of inhibitors of α-synuclein fibrils.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: National Institutes of Health (NIH); USDOE

Grant/Contract Number:: AC02-06CH11357; AC02-05CH11231; FC02-02ER63421; NIH-AG016570

OSTI ID:: 1222837

Alternate ID(s):: OSTI ID: 1513790

Journal Information:: Nature (London), Vol. 525, Issue 7570; ISSN 0028-0836

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 430 works

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