Extended Data Fig. 2: Cryo-EM processing and 3D reconstruction workflow.
From: Structures of human mGlu2 and mGlu7 homo- and heterodimers
a–f, Results of the inactive mGlu2 homodimer. a, Processing workflow. b, Representative cryo-EM image from four independent experiments with similar results. c, Two-dimensional averages. d, Cryo-EM map coloured according to local resolution (in Å). e, Gold-standard Fourier shell correlation (FSC) curve showing an overall resolution at 3.6 Å. f, Cross-validation of model to cryo-EM density map. FSC curves for the final model versus the final map and half maps are shown in black, red and green, respectively. g–l, Results of the inactive mGlu7 homodimer. g, Processing workflow. h, Representative cryo-EM image from five independent experiments with similar results. i, Two-dimensional averages. j, Cryo-EM map coloured according to local resolution (in Å). k, Gold-standard FSC curves showing an overall resolution at 4.0 Å and a resolution at 3.6 Å for the extracellular domains (ECDs). l, Cross-validation of model to cryo-EM density map. m–r, Results of the agonist- and PAM-bound mGlu2 homodimer. m, Processing workflow. n, Representative cryo-EM image from three independent experiments with similar results. o, Two-dimensional averages. p, Cryo-EM map coloured according to local resolution (in Å). q, Gold-standard FSC curve showing an overall resolution at 3.1 Å. r, Cross-validation of model to cryo-EM density map. s–x, Results of the inactive mGlu2–mGlu7 heterodimer. s, Processing workflow. t, Representative cryo-EM image from four independent experiments with similar results. u, Two-dimensional averages. v, Cryo-EM map coloured according to local resolution (in Å). w, Gold-standard FSC curves showing an overall resolution at 3.9 Å and a resolution at 3.5 Å for the extracellular domains. x, Cross-validation of model to cryo-EM density map.
