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![[Figure 4]](wa5105fig4mag.jpg)
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Figure 4
Electron-density maps of ligands bound to PepTSt and β2AR in crystal structures solved by the IMISXcryo method at resolutions of 2.4 and 2.5 Å, respectively. (a, b) Views into the peptide-binding pocket of PepTSt reveal the dipeptide Ala-Phe in well defined density. (c, d) Views into the ligand-binding pocket of β2AR reveal the partial inverse agonist carazolol in well defined density. Ligands are shown with yellow C atoms and with an Fo − Fc map (green mesh) contoured at 3σ. 2Fo − Fc maps are contoured at 1σ (blue mesh). Relevant residues are highlighted as sticks with grey C atoms. The protein backbone is shown in thin ribbon representation coloured green. Helices (H) and an extracellular loop (ECL) are indicated following the notation in the original literature. Stick models include N (blue) and O (red) atoms. |
![[Figure 4]](wa5105fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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