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. Author manuscript; available in PMC: 2012 Feb 9.
Published in final edited form as: Structure. 2011 Feb 9;19(2):155–161. doi: 10.1016/j.str.2010.12.007

Figure 4. Cross-crystal averaging in the antibody region improves electron density map in the gp120-CD4 region in the gp120-CD4-antibody complex crystal.

Figure 4

(A) Part of the electron density map in the gp120 region after rigid-body refinement and before averaging. (B) The same region after cross-crystal averaging. (C) Automated model building of the entire gp120 and CD4 domains based on the averaged map. The final models of the gp120 and CD4 are shown in blue, and the automatically-built skeleton is shown in red. (D) Changes of ρ/σ in the gp120-CD4 region during the averaging process. (E) Changes of the map correlation coefficients in the gp120-CD4 region during the averaging process.