Extended Data Fig. 3: Cryo-EM images and single-particle reconstruction of the Org43553–CG–LHCGR(WT)–Gs complex and inactive LHCGR, and electron microscopy maps for the inactive LHCGR structure.
From: Structures of full-length glycoprotein hormone receptor signalling complexes
a, b, Size-exclusion chromatography elution profiles and SDS-PAGEs of the Org43553–CG–LHCGR(WT)–Gs complex (left panel) and inactive LHCGR (right panel). Red stars indicate the monomer peaks of the two proteins. For gel source data, see Supplementary Fig. 1 (Experiments were repeated three times with similar results). c, d, Cryo-EM micrograph, reference-free 2D class averages, and flowchart of cryo-EM data analysis of the Org43553–CG–LHCGR(WT)–Gs complex (c) and inactive LHCGR (d). e, f, Cryo-EM maps of the Org43553–CG–LHCGR(WT)–Gs complex (e) and inactive LHCGR (f) coloured by local resolutions from 2.0 Å (blue) to 5.0 Å (red). The “Gold-standard” Fourier shell correlation (FSC) curves indicate that the overall resolution of the electron density map of the Org43553–CG–LHCGR(WT)–Gs complex is 4.3 Å (e) and inactive LHCGR is 3.8 Å (f). g, Cryo-EM density map and model of the inactive LHCGR. The regions of the cryo-EM density map with all transmembrane helices and H8 are shown.
