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. 2020 Oct 1;10:16293. doi: 10.1038/s41598-020-73207-9

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Maximum and average number of binding of various metal ions (in bold) to the 8+ charge state of α-syn. Per metal salt four bars are shown which correspond to protein:metal ion ratios of 1:1, 1:4, 1:50 and 1:250 from left to right. The height of each bar indicates the maximum number of metal ions bound (S/N ≥ 3), and the dot in each bar corresponds to the average metal binding (weighted peak intensities of all stoichiometries detected, including the unbound state when present). In cases where it was difficult to determine the stoichiometry due to poorly resolved signal, an asterisk* is shown. When no binding of metal ions was observed, ‘0′ is shown.