Extended Data Fig. 4: Cryo-EM processing scheme from structure representing TRIP12ΔN forming a branched K29/K48-linked ubiquitin chain. | Nature Structural & Molecular Biology

Extended Data Fig. 4: Cryo-EM processing scheme from structure representing TRIP12ΔN forming a branched K29/K48-linked ubiquitin chain.

From: TRIP12 structures reveal HECT E3 formation of K29 linkages and branched ubiquitin chains

Extended Data Fig. 4

a, Processing scheme. Scalebar on micrograph corresponds to 500 Å. Data processed in Cryosparc 4.5.3 yielded a 3D reconstruction with a resolution of 3.7 Å by the gold-standard Fourier shell correlation of 0.143. b, Gold-standard Fourier shell correlation plot. c, Orientation distribution plot of particles from final refinement. d, Local resolution estimation projected onto deepEMhancer-sharpened map.

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