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The application of X-ray crystallography and site-directed mutagenesis to the study of protein structures

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The application of X-ray crystallography and site-directed mutagenesis

to the study of protein structures

Thomassen, Ellen Anna Johannes

Citation

Thomassen, E. A. J. (2005, April 28). The application of X-ray crystallography and

site-directed mutagenesis to the study of protein structures. Retrieved from

https://hdl.handle.net/1887/834

Version:

Corrected Publisher’s Version

License:

Licence agreement concerning inclusion of doctoral thesis in the

Institutional Repository of the University of Leiden

Downloaded from:

https://hdl.handle.net/1887/834

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150

Figure 3.10. Superposition of the Calpha atoms (amino acid 468-477) of a part of the "bonnet"of the two gp12 trimers in different space groups. a) Top view on the bonnet along the three-fold axis. Both gp12 trimers in different colors, R32 (blue) and P321 (green). b) Rotated 90 degrees, same colors as in a). It shows clearly that the top region of the receptor-binding domain, the "bonnet", has differences in the main-chain positions for the residues 469-479.

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