Extended Data Fig. 7: Cryo-EM processing flowchart for CUL9-RBX1ΔCPH, CUL9-RBX1ΔARIH-RBR, CUL9-RBX1ΔARM9 and CUL9-RBX1ΔDOC. | Nature Structural & Molecular Biology

Extended Data Fig. 7: Cryo-EM processing flowchart for CUL9-RBX1ΔCPH, CUL9-RBX1ΔARIH-RBR, CUL9-RBX1ΔARM9 and CUL9-RBX1ΔDOC.

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

Extended Data Fig. 7

a, Representative micrograph and cryo-EM processing scheme for CUL9-RBX1ΔCPH, in which CPH domain was replaced by a linker of sequence GSGSGSGS. b, Representative micrograph and cryo-EM processing scheme for CUL9-RBX1ΔARM9, in which ARM9 domain was replaced by a linker of sequence GSGSGSGS. c, Representative micrograph and cryo-EM processing scheme for CUL9-RBX1ΔARIH-RBR, a variant lacking ARIH-RBR element by truncation at residue 1978. d, Representative micrograph and cryo-EM processing scheme for CUL9-RBX1ΔDOC, in which DOC domain was replaced by a linker of sequence GSGSGSGS.

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