X-ray diffraction analysis for determination of the three-dimensional structure of proteins at an atomic level is an essential method within structural biology. Numerous issues within fundamental science as well as in the context of special applications can be answered with a protein structure.
- solving of catalytic mechanisms,
- identification of amino acids suited for specific mutagenesis (protein engineering),
- visualisation of protein-ligand-interactions, e. g. for determination or development of appropriate inhibitors/activators,
- insights in structure-properties relationships for proteins or protein mutants involved in disease patterns.
To determine the three-dimensional structure of a protein by means of x-ray diffraction analysis the first and major crucial step is the generation of a highly ordered single crystal of the corresponding protein. This prerequisite marks the starting point of a labour-intensive, sometimes tedious, empirical process: the search for a suited crystallization condition. Having overcome that hurdle several complex steps follow in order to verify and optimize these first crystals before they are applicable for data collection.
The CSS as research- and service center provides all these essential working steps as full-service for all members of the HHU as well as for external users: starting with the search for initial crystallization conditions, followed by crystal optimization, data collection at synchrotrons and structure determination and refinement.