1. komponenta

Lecture type	Total
Lectures	30
Practicum	15
Seminar	15

* Load is given in academic hour (1 academic hour = 45 minutes)

LEARNING OUTCOMES:
1. Explain the principles of diffraction on crystals.
2. Explain methods for X-ray crystal structure determination.
3. Perform the experiment of protein crystallization.
4. Apply the basic methods of solving and refining protein structures.
5. Use databases of solved protein structures.

LECTURES:
1. Macroscopic properties of crystals.
2. Symmetry in crystals; Miller indices and point groups.
3. Crystal lattices.
4. Space groups.
5. Basic principles of diffraction on single crystals; Bragg's law.
6. Methods of crystallization of proteins.
7. X-ray sources and detectors.
8. Fourier synthesis; phase problem.
9. Diffraction data collection.
10.Protein databases.
11. Basic methods of protein crystal structure solving.
12. Building of the model and refinement.
13. Analysis of the structure.

SEMINARS:
Independent solving, refining, analyzing, and visualizing the assigned structure of the biological macromolecule and presenting the solution.

EXPERIMENTAL WORK:
1. Crystallization of selected protein by vapour diffusion technique (hanging drops).
2. Crystal mounting and data collection.
3. Data processing and structure determination using the molecular replacement method.
4. Structure refinement.
5. Structure analysis and molecular graphics.

1. Biomolecular Crystallography: Principles, Practice, and Application to Structural Biology, Bernard Rupp, New York, Garland Science, 2009.
2. Principles of Protein X-Ray Crystallography, Jan Drenth, 3rd Ed, Springer, 2007.
3. Crystal Structure Determination, W. Clegg, Oxford University Press, Oxford, 2002.
4. Fundamentals of Crystallography, Carmelo Giacovazzo (ed.), Carmelo Giacovazzo, Hugo Luis Monaco, Gilberto Artioli, Davide Viterbo, Marco Milanesio, Gastone Gilli, Paola Gilli, Giuseppe Zanotti, Giovanni Ferraris, Michele Catti, 3rd Ed, Oxford Academic, 2011.

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