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. Author manuscript; available in PMC: 2013 Nov 30.
Published in final edited form as: Nature. 2013 May 30;497(7451):643–646. doi: 10.1038/nature12162

Figure 2. Mutational analysis of the hydrophobic trimer interface.

Figure 2

a, Detailed viewof the trimer interface, with the structural model superimposed on the density map (grey mesh, contoured at 3.5σ). Selected residues are depicted in stick-and-ball representation. b, Virus infectivity (blue) and capsid stability (black), as percentage of total CA,± standard deviation (n=53), of wild-type (WT) and CA trimer interface mutants. c, Spontaneous disulphide crosslinking of A204C mature and maturation-defective virions analysed by immunoblotting for CA. d, In vitro assembly of recombinant wild-type and A204C CA proteins, assayed with high-speed sedimentation and polyacrylamide gel electrophoresis analysis. Letters u, s and p denote the unassembled reaction mixture (u) and the supernatant (s) and pellet (p) after assembly. e, Cryo-EM image of A204C in vitro assembly. Scale bar, 100 nm.