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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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149 (a) (b) (c) His445 His447 His445 His447 His447 His445 His447 His445 His445

Figure 3.5. Possible LPS binding residues. b) Electron surface potential of the trimer. Positive

charges are marked in blue, negative in red. Putative receptor-binding amino acids (see text) are labelled. Please note that although the five labelled residues appear to cluster in two groups, they are in fact all very close to each other due to the 3-fold symmetry. c) Surface diagram showing in green aromatic amino side-chains that may be involved in LPS binding. Labels identify the amino acids. The protein is tilted forwards to afford a better view of the top of the trimer. Residues are labelled by their one-letter amino acid code.

Figure 3.6. The zinc ion in the centre of the receptor-binding domain. Shown here are the main

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