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. Author manuscript; available in PMC: 2016 Jul 30.
Published in final edited form as: Cell. 2015 Jul 16;162(3):493–504. doi: 10.1016/j.cell.2015.06.057

Figure 2. scFv Ab513-EDIII (DENV-4, BC287/97 (Mexico/1997)) Complex Structure.

Figure 2

(A–D) The asymmetric unit of crystal forms I (A) and II (B) contain six and two Ab513-EDIII complexes, respectively. The scFvs of form I are rendered in solvent accessible surface format and the EDIII domains are rendered in cartoon format. The interface formed by the heavy chains of the two ScFvs in the dimer is shown in C. (D) Comparison of the antibody-EDIII interface for Ab513 (left) and 4E11 (right) demonstrating that deletion of Ser26 results in higher surface complementarity due to removal of the “elbow” present in 4E11.