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. Author manuscript; available in PMC: 2014 May 26.
Published in final edited form as: Nucl Med Biol. 2010 Oct 27;38(2):223–233. doi: 10.1016/j.nucmedbio.2010.08.013

Fig. 3. Mutations resulting from affinity maturation.

Fig. 3

Mutations accrued through eight rounds of affinity maturation are highlighted in blue in the x-ray crystal structure of the 2D12.5 Fab (A) and a magnified view of the binding pocket (B). Panels A and B were generated with PyMol based on the research collaboration for structural bioinformatics (RCSB) protein data bank entry 1NC2 [38]. Panel C shows the sequence alignment of the 2D12.5ds and C8.2.5 scFvs. Residues within 5 Angstroms of the hapten from the 2D12.5 crystal structure are highlighted in yellow; the (Gly4Ser)3 linker is highlighted in grey. Note that the residue numbering is different from that for the crystal structure of the Fab.