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. 2021 Nov 8;11:21787. doi: 10.1038/s41598-021-00236-3

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© The Author(s) 2021

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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Electron density of selected regions of the PS I protein complex derived from the 2.75 Å resolution room temperature diffraction data. (a) A portion of a transmembrane alpha-helix (PsaB576–PsaB591) with side chains modeled into 2F_obs− F_calc electron density contoured to 1.5 $σ$ . Side chains are clearly visible in this region of the map. (b) Electron density in the region of the special pair P700 formed by a Chl a (labeled P_B) and a Chl a’ (labeled P_A). Mg²⁺ coordinating His residues and the Chls are shown as sticks, the 2F_obs− F_calc electron density is shown as blue mesh contoured at 1.5 $σ$ . Figure generated with Pymol v. 2.4.0a0, https://pymol.org.