Fig. 1: Cryo-EM structure reveals hexameric CUL9–RBX1 E3 ligase complex. | Nature Structural & Molecular Biology

Fig. 1: Cryo-EM structure reveals hexameric CUL9–RBX1 E3 ligase complex.

From: Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex

Fig. 1

a, Cryo-EM map of CUL9–RBX1 after 3D refinement, calculated with C3 symmetry and low-pass filtered to 10 Å resolution. b, Cryo-EM reconstruction of hexameric CUL9–RBX1 refined to 4.4 Å resolution (calculated with C3 symmetry and postprocessed with DeepEMhancer). Individual CUL9 protomers are color-coded. c, Structure of hexameric CUL9–RBX1 aligned with orientation of cryo-EM map as in b. d, Representative 2D classes of CUL9–RBX1. Scale bar, 250 Å. e, Mass photometry analysis of purified CUL9–RBX1. Calc., calculated; MW, molecular weight. f, Immunoblot of CUL9 from sucrose gradient fractions of purified hexameric CUL9–RBX1 or endogenous CUL9 from U2OS cells (n = 3 technically independent experiments).

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