pbio.3001295.s002.tif (5.74 MB)

Local resolution and atomic modelling into the cryo-EM density maps.

figure

posted on 2021-06-04, 18:27 authored by Jesse I. Mobbs, Matthew J. Belousoff, Kaleeckal G. Harikumar, Sarah J. Piper, Xiaomeng Xu, Sebastian G. B. Furness, Hari Venugopal, Arthur Christopoulos, Radostin Danev, Denise Wootten, David M. Thal, Laurence J. Miller, Patrick M. Sexton

Local resolution of (A) the consensus map, (B) G protein–focused refinement, and (C) receptor-focused refinement of the CCK-8/CCK1R/mGαsqi/Gβ1γ2/scFv16 complex. (D) Density maps and models are illustrated for all 7 transmembrane helices and ECL2 of CCK1R, the αH5 of the Gα subunit, and the CCK-8 peptide. (E, F) Local resolution of the consensus (E) and receptor-focused (F) maps for the CCK-8/CCK1R/DNGαs/Gβ1γ2/Nb35 complex. (G) Density maps and models are illustrated for all 7 transmembrane helices and ECL2 of CCK1R, the αH5 of the Gα subunit, and the CCK-8 peptide. Protein backbone is displayed in ribbon format with amino acid side chains in stick representation, coloured by heteroatom. The cryo-EM density was zoned at 1.8 Å. αH5, α5 helix; CCK, cholecystokinin; CCK1R, cholecystokinin type 1 receptor; cryo-EM, cryo-electron microscopy.

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