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. 2019 May 6;9:6969. doi: 10.1038/s41598-019-43360-x

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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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Conformational landscape of the dimer interface at the agonist-binding domain at site 479 in full length homomeric GluK2 receptors. Representative smFRET traces and FRET histograms showing fractional occurrence as a function of FRET efficiency in presence of 150 mM CsCl in the (A) apo state (data from 55 molecules), (B) presence of 1 mM glutamate (data from 52 molecules), and (C) D776K mutant in the presence of 1 mM glutamate (data from 55 molecules).