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Load:
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1. komponenta
| Lecture type | Total |
| Lectures |
30 |
| Seminar |
15 |
* Load is given in academic hour (1 academic hour = 45 minutes)
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Description:
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COURSE CONTENT:
X-ray sources, basics of symmetry, crystal lattice, crystallization techniques, diffraction and intensity of diffraction maxima. Comparison of different experimental methods used in structure solving procedures. Phase problem, the role of Fourier transforms and convolution in structure solving, structure refinement, geometry analysis and presentation of solved crystal and molecular structures.
LEARNING OUTCOMES:
1. Explaining advantage/disadvantage of X-ray structure analysis for specific samples in comparison to other diffraction methods (neutron and electron diffraction).
2. Describing sources and detectors of X-rays, neutrons and electrons.
3. Usage of the basic concepts of symmetry, crystal lattice, diffraction and intesities of diffracted maxima.
4. Describing the problem of phases.
5. Collection of diffraction data, solving and refining crystal structures and their graphical presentation by using the appropriate programs.
6. Searching crystallographic databases
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Literature:
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- 1. C. Giacovazzo et al.: Fundamentals of Crystallography, 2. izdanje, Oxford Univ. Press, Oxford 2002.
- 2. Jan Drenth: Principles of Protein Crystallography, 3. izdanje, Springer Science, 2007.
- 3. I. Vicković: Difrakcijske metode određivanja kristalnih struktura, interna skripta, 1996.
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Pristupačnost
