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. 2010 Mar 2;19(5):954–966. doi: 10.1002/pro.372

Figure 5.

Figure 5

Identification of intermolecular CDR contacts in the IgG2 Fab2 crystal structure. The eight Fabs in the asymmetric unit of the Fab2 structure, designated A/B, C/D, E/F, G/H, I/J, K/L, M/N, and O/P (LC/HC), displayed two types of packing interactions. (A) Stereo electron density at 1 sigma of the cluster of hydrophobic CDR residues that formed intermolecular contacts. (B) Crystal packing of CDR–CDR contacts of Fab A/B with Fab E/F, highlighting residues considered for targeted mutagenesis. HC residues I57, W104, P53, and W94 are in pink and blue, and LC W94 in green and yellow. (C) Crystal packing of the CDR-framework interactions of the J chain CDRs (blue) of Fab I/J with F chain (pink) framework residues G8-G10 and K76 of Fab E/F.