Extended Data Fig. 2: Representative structural determination of hDAT^DA.

a, Cryo-EM data processing flowchart of hDAT^DA. Representative micrograph of hDAT^DA was shown with the white scale bar equaling 100 nm. Briefly, 3,862,637 particles were picked from 6,138 collected movies. After several rounds of 2D classification, an initial map was reconstructed by ab-initio reconstruction. The initial map then severed as a reference for heterogeneous refinement of all particles. Following two more rounds of ab-initio reconstruction and non-uniform refinement, the map resolution was improved to 3.06 Å. The final map (2.80 Å) was obtained through 3D classification without alignment and local refinement. Particles and resolutions at each stage of data processing are labeled. For details, refer to ‘Cryo-EM data analysis’ section in the Methods. b, Local resolution distribution of the final map of the hDAT^DA. c, Euler angle distribution of the 3D reconstruction for hDAT^DA. d, Gold-standard Fourier Shell Correlations (FSC) curves of model versus map (black), unmasked map (blue) and masked map (red), marked with resolutions corresponding to FSC = 0.5 and 0.143. e, Cryo-EM densities superimposed on atomic model of the 12 transmembrane helices of hDAT^DA.