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![[Figure 7]](jb5013fig7mag.jpg)
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Figure 7
The C-terminal tag-cleavage remnants drive multiple crystal forms though β-extension packing in crystal contacts. (a) Ribbon and stick representation showing the C-terminal tag remnants forming a β-sheet extension with a symmetry-related molecule in the P21 crystal form (PDB entry 6qf9) grown from PEG 4000 (resolution 1.4 Å). The inset shows the overall packing. (b) Ribbon and stick representation showing the C2 crystal form of the scFv (PDB entry 6qb9; resolution 1.85 Å) grown from tartrate. The inset shows the overall packing. (c) N-terminally tagged and cleaved E. coli-scFv crystal structure in space group P43212 showing four monomers in the asymmetric unit (PDB entry 6qf6; resolution 2.6 Å). (d) Surface representation of the scFv CDR region of PDB entry 6qb9 with the two tartrate molecules from the crystallization solution shown as sticks. Overlaid in orange is the Mcl-1 epitope from the complex structure shown as a Cα trace. Asp313 and Glu317 normally occupy the tartrate-binding sites in the complex (shown as side-chain sticks). |
![[Figure 7]](jb5013fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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