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:
Different topics, such as: crystallization of membrane proteins; small-angle X-ray scattering in structural biology; X-ray powder diffraction in structural biology; NMR structure determination of proteins; Neutron crystallography.
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. C. Giacovazzo, H. L. Monaco, G. Artioli, D. Viterbo, G. Ferraris, G. Gilli, G. Zanotti, M. Cati, Fundamentals of Crystallography, 2nd Ed, Oxford University Press, 2002
2. Jan Drenth, Principles of Protein X-Ray Crystallography, 3rd Ed, Springer 2007
3. W. Clegg, Crystal Structure Determination, Oxford University Press, Oxford, 2002

Izborni predmeti - Strukturna biologija - Regular study - Molecular Biology