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. 2017 Sep 14;8:542. doi: 10.1038/s41467-017-00630-4

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© The Author(s) 2017

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. 6 — Comparison of the A_2A receptor electron density obtained using SMX, SFX and conventional cryo-crystallographic data. The structures show the ligand binding pocket with 2F_o–F_c maps shown at 1σ. All data sets were collected using A_2AR crystals prepared in the same way to facilitate a direct comparison of the techniques. The SMX density is well defined, but the overall resolution (2.1 Å) is lower than in SFX (1.7 Å) and cryo-crystallography (1.95 Å)