At the end of the course, you should be able to:
- Perform all steps of a standard protein crystal structure determination by molecular replacement using the crystallographic software package CCP4.
- Interpret relevant quality indicators in each step of the structure determination process.
- Evaluate the quality of published models from protein crystallography.
- Judge whether a conclusion based on a crystal structure is justified considering the quality of the diffraction data.
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X-ray diffraction on protein crystals is a powerful technique to determine structures of large biomolecules at (near) atomic resolution. Technological and methodological advances and the vast and steadily increasing number of protein structures already available, enable rapid determination of protein structures by the method of molecular replacement, provided that suitable diffracting crystals can be obtained and the structure of a >25% homologous protein is available. In this hands-on course you will determine a protein crystal structure yourself using molecular replacement. You will perform all steps from diffraction data processing to validation and analysis of the refined model.
The objectives of the course are two-fold: firstly to learn how to obtain the best possible protein model by making informed decisions on the basis of relevant quality indicators throughout the structure determination process. Secondly, to learn how to critically judge the quality of protein structures from the protein data bank and their suitability as a starting point for further research. In fact solving a protein structure yourself is an excellent way to appreciate the strengths and pitfalls of protein crystal structures. The course aims at students that wish to be able to determine crystals structures themselves as well as students that wish to be able to use the wealth of information that protein structures provide in a critical fashion. The underlying physics and mathematics of X-ray crystallography will be dealt with in a qualitative manner and only for as far it is relevant for the quality of the final protein model. A typical course day consists of a lecture, computer practical (with and without guidance), and student presentations about the progress of their structure determinations.
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