Extended Data Fig. 3: Cryo-EM data analysis of Saccharomyces cerevisiae Erf2-Erf4 complex.
From: Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation
a, A representative cryo-EM. Scale bar: 50 nm. b, Representative two-dimensional class averages. Box size: 209 Å; Circle mask: 177 Å. Scale bar: 5 nm. c, Angular distribution of the particles of the final map reconstruction generated by cryoSPARC. d, Gold standard Fourier shell correlation (FSC) curves for the 3D reconstructions generated by cryoSPARC. The curves representing the corrected (random phase initialized), tight mask, loose mask and no mask are colored black, red, blue, and orange respectively. e, Validation of the final structure model. The curves indicate the FSC of the model versus the overall map/ half map 1/ half map 2 (FSC = 0.5). f, A flowchart of EM data processing. Please refer to ‘Cryo-EM image processing’ section in Methods for details. The map labelled ‘good reference’ was used to repick particle coordinates and further refinement. The map labelled ‘final map’ was applied to build and refine the atomic model subsequently. The 3D classes in grey dashed boxes were considered as good classes which were selected during the processing steps.
