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. 2019 Jun 25;9:9210. doi: 10.1038/s41598-019-45545-w

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© The Author(s) 2019

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Early oligomeric states of CRES. (a) Coomassie Blue stained SDS-PAGE gel of purified CRES showed a single band at approximately 14 kDa. (b) DLS analysis of four different CRES preparations (Prep 1–4) (~11–16 μM) in high salt gel filtration buffer. Intensity measurements showed populations of CRES particles at 4–8 nm and 400–1000 nm. Inset, an average hydrodynamic radius for the particles between 4–8 nm was calculated from the fitted data and diameter ± SD is reported. Due to large variations in particle size we were unable to fit the CRES particles between 400–1000 nm. (c) Negative stain TEM showed CRES was present as granular structures (top panel) with some oligomeric/protofibril amyloid forms (bottom panel). Data are representative of n = 4 CRES preparations. (d) CD analysis of ~11–16 μM CRES exchanged into 4 mM potassium phosphate buffer indicated a protein with mixed secondary structure. CD spectral curve shows experimental (dotted line) and fitted data (solid line) from a representative CRES preparation. Table shows the mean ± SEM secondary structure as predicted from the spectral data by the BeStSel server from n = 3 independent CRES preparations.