Extended Data Fig. 1: Cryo-EM sample preparation, data collection and processing for APJRcmpd644-Gi-scFv16. | Nature Structural & Molecular Biology

Extended Data Fig. 1: Cryo-EM sample preparation, data collection and processing for APJRcmpd644-Gi-scFv16.

From: Structural insight into apelin receptor-G protein stoichiometry

Extended Data Fig. 1

a, Representative cryo-EM image from 7,337 micrographs of the APJRcmpd644-Gi-scFv16 complex. Scale bar, 50 nm. b, Representative 2D averages showing distinct secondary structural features from different views of the complex. c, Cryo-EM data processing workflow. The data was all processed by CryoSPARC and images of density maps were created in UCSF Chimera. The final 3D density maps are colored according to the local resolution. Gold-standard FSC curves from Phenix indicate overall nominal resolutions of 3.57 Å and 3.71 Å using the FSC = 0.143 criterion for the dimAPJRcmpd644-Gi map (light blue curve, left) and monAPJRcmpd644-Gi map (dark blue curve, right), respectively. d, Elution profile and gel image of APJR (comprising residues 1–350), Gαi, Gβ, Gγ and scFv16 after SEC purification. The collected fraction for cryo-EM sample were marked between dashed lines.

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