Methods of Protein Crystallography

Type of instruction




Part of degree program


Recommended in

Semesters 1-4

Typically offered in

Autumn/Spring semester

Course description

Introduction to X-ray diffraction, the methods of structure determination of biological macromolecules. A practical approach.

1. Theoretical background, possible implications and limitations;

2. The electron density function and the structure factor. (Diffraction of X-rays on a crystal lattice; The crystallographic phase problem; Symmetry);

3. Crystallization and data collection strategies;

4. Solving the phase problem (The Patterson function; Molecular replacement; Isomorphous replacement methods; Use of anomalous dispersion);

5. From electron density maps to 2D structure of the molecule: model building and refinement. (The model bias);

6. Validation of the refined model;

7. New directions and challenges in protein crystallography (Structural genomics; Large structures and poor crystals);

8.Applications in drug discovery (Structure based and fragment based drug design);

9. Mebmrane proteins;

10. A molecular movie: time resolved crystallography

  •  Gale Rhodes: "Crystallography Made Crystal Clear; A Guide for Users of Macromolecular Models", Academic Press 2006

  • Blow, David „Outline of Crystallography for Biologists”, Oxford University Press 2002

  • Drenth, Jan „Principles of Protein X-Ray Crystallography” Springer 1999