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. 2022 Apr 20;605(7908):172–178. doi: 10.1038/s41586-022-04637-w

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© The Author(s) 2022

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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Fig. 2 — a, Particles of GluA2–γ2 collected at 20 µM Glu and 100 µM CTZ produced an average three-dimensional reconstruction (left) and classified on the basis of the LBD layer (light green) and focused on the LBD–TMD (red contour) into seven structures (right). GluA2 subunits not bound to Glu (N) are shown in blue, Glu-bound (G) in pink and γ2 in dark green. b, c, Side views of monomers (b) and dimers (c) of LBD that represent the GluA2–γ2 structural ensemble at low Glu concentration. Glu molecules are shown in ball-and-stick representation (yellow), whereas CTZ (green) and disulfide-linked cysteines C718 and C773 are shown as sticks. LBD clamshell closure in response to Glu binding is indicated by red arrows. d, Top views of LBD tetramers that represent the GluA2–γ2 structural ensemble are shown in surface representation and viewed from the ion channel side.