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Lecturer(s)
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Kutá Smatanová Ivana, prof. Mgr. Ph.D.
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Schneider Bohdan, prof. Ing. CSc.
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Kužel Radomír, prof. RNDr. CSc.
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Course content
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Content of lectures: 1. Fundamentals of crystallography - directions and planes, symmetry operations, point groups and their importance, plane and space groups, International tables of crystallography 2. Basic physical and chemical crystallography 3. X-ray diffraction, scattering radiation on electrons, atoms, molecules and crystal, atomic and structure factor 4. Powder diffraction and its possibilities, phase analysis, Rietveld method 5. Other methods of X-rays scattering - analysis of thin layers, small-angle scattering, modern imaging methods 6. Introduction to protein crystallography, crystal types, parameters influencing crystallizing of biomolecules 7. Standard, advanced and alternative methods of crystallization 8. Testing crystals and preparing crystals for diffraction experiment 9. Crystallographic experiment: a radiation source, measuring diffraction data on laboratory and synchrotron sources 10. Data processing, symmetry and solving the phase problem 11. Structure refinement 12. Biomolecular structures archives, structural databases and their use. Structure validation. Content of practicals: During exercises students will theoretically learn about practical application of crystallization techniques, the work with the crystallization robot, measuring crystals on home-source diffractometer, as well as the basics of the diffraction data collection and their use to determine the molecular structure. It will also be practicing the use of structural databases and structure validation.
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Learning activities and teaching methods
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Monologic (reading, lecture, briefing), Dialogic (discussion, interview, brainstorming), Work with text (with textbook, with book), Monitoring, Demonstration, Activating (simulations, games, drama), Excursion
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Learning outcomes
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Lectures will clarify students the latest knowledge and trends in the fields of protein crystallography and powder diffraction. Students will become familiar with the preparation of protein crystals and material samples, a diffraction experiment and evaluation of the diffraction data. Briefly, the physical background of mentioned methods will be explained.
Students will be introduced during the lectures with selected experimental methods - powder and protein crystallography, which are used in structural and functional studies of proteins and macromolecular complexes.
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Prerequisites
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Minimal requirement for students is basic knowledge of all chemistry and knowledge of biochemistry.
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Assessment methods and criteria
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Student performance assessment, Interview, Combined exam
The requirement for successful completion of the course is the active participation of students in seminars. The final exam will take the form of an oral / written test in each field and a subsequent oral interview with a final evaluation in the form of awarding an average grade proposed by all examiners.
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Recommended literature
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B. Rupp: Biomolecular Crystallography: Principles, Practice, and Application to Structural Biology. Garland Science, New York (2009).
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Bergfors, T., Editor. Protein Crystallization: Second Edition. International University Line, La Jolla, CA, USA 2009.
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G. Rhodes: Crystallography made crystal clear. Elsevier, Amsterdam (2006)..
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J. Drenth Principles of Protein X-ray Crystallography, Springer Verlag Publishing, USA 2002.
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R. Giege A. Ducruix and Crystallization of NA and Proteins, A Practical Approach, Oxford University Press, NY USA 1992..
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