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. 2020 Dec 10;60(6):3131–3137. doi: 10.1002/anie.202011793

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© 2020 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Nearly identical conformations of rCa_v1.1 in the presence of DHP compounds in detergents and in nanodiscs. A) Overall structure of the amlodipine‐bound rCa_v1.1 complex (rCa_v1.1‐100A) at 2.9 Å resolution. The overall structure of the channel complex is colored for different subunits. The β1 subunit is omitted throughout the manuscript because of its poor resolution. Amlodipine is shown as orange spheres and the bound lipids are shown as gray sticks. The approximate position of the membrane is indicated by black lines. B) The structures of rCa_v1.1‐100A (with 100 μm amlodipine, pink) and rCa_v1.1‐100R (with 100 μm RBK, cyan) in nanodiscs and rCa_v1.1‐200N (with 200 μm nifedipine, gray) in digitonin are nearly identical. C) Structures of rCa_v1.1‐100S (with 100 μm SBK) in nanodisc (green) and in digitonin (light purple) are nearly identical.