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. 2019 Jun 12;25(6):873–883.e5. doi: 10.1016/j.chom.2019.04.011

Figure 2.

Figure 2

Cryo-EM Reconstruction of Env Trimer AMC011 SOSIP.v4.2 in Complex with bnAb ACS202

(A) Reconstruction of Env trimer AMC011 SOSIP.v4.2 in complex with ACS202 Fab at ∼5.2 Å resolution, segmented to highlight densities corresponding to gp120 (yellow), gp41 (white), and ACS202 Fab (blue).

(B) Model of Env trimer AMC011 SOSIP.v4.2 in complex with ACS202 Fab. Glycans are shown as green spheres. The FP is shown in yellow. Variable domains of ACS202 are shown in dark (heavy chain) and light (light chain) blue.

(C) Crystal structure illustrating the interaction between ACS202 (blue) and synthetic FP fragment (green).

(D) Cryo-EM structure shows that the interaction between ACS202 and the FP region (yellow) of Env trimer AMC011 SOSIP.v4.2 is similar to that with the synthetic FP, as shown in (C). The root-mean-square deviation (RMSD) (Cα) between the FPs is 1.7 Å.

(E) Detailed interactions of Fab ACS202 recognition of AMC011 SOSIP.v4.2 Env trimer. Glycans are shown as green spheres. Side chains of the FP (yellow) are shown in sticks. Interactions between CDRH2 of ACS202 and the Env trimer are highlighted in the top right corner.

See also Figure S4 and Table S3.