COURSE DESCRIPTION: X-ray diffraction studies of single crystals as a tool for structure determination of biologically important molecules is described: Crystallization of small molecules and proteins: evaporation, diffusion, dialysis, preparation of crystals for diffraction experiments. Diffraction of X-rays by crystals: reciprocal space, structure factors, symmetry, single crystal diffractometer, data collection and processing. Structure determination and refinement methods for small molecules, interpretation of results, Cambridge Structural Database. Structure determination and refinement methods for proteins: molecular replacement, MIR, MAD refinement, simulated annealing method, analysis of Fourier maps. Structure validation, Protein Data Bank.

OBJECTIVE OF THE COURSE:
The aims of this unit are:

• To develop the competence of the student for using X-ray diffraction methods to determine structure of small molecules and proteins
• To highlight modern advances in diffraction methods
• To show the students how the X-ray crystallography results can be applied in chemistry

INTENDED LEARNING OUTCOMES:

After completing this unit students should be able to cope with:

• Problems in obtaining quality crystals
• Identification of problems in crystal structure determination process
• Application of structural data bases and literature in chemistry and biochemistry

TEACHING AND LEARNING ACTIVITIES:

Lectures and exercises: 50 hours

Student centered learning: 70 hours; Total student effort: 120 hours

LANGUAGE OF INSTRUCTION: English

RECOMMENDED READING:

Crystal Structure Analysis for Chemists and Biologists Jenny P. Glusker, Mitchell Lewis, Miriam Rossi
Outline of Crystallography for Biologists. David Blow

RECOMMENDED WEBSITES:  www.iucr.org/cww-top/edu.index.html

SCHEDULE AND LEARNING METHOD:

ASSESSMENT:

Written protocol with the correct structural elucidation for a given problem (25%). Written final examination (75%)

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