Entry requirements

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Aims

The course is an introduction to macromolecular X-ray crystallography in general, and protein crystallography in particular.

Understanding macromolecular function and underlying molecular structures. X-ray crystallography is the most powerful contemporary technique available to provide detailed structural information of these structures.

Content

The course provides an introduction to crystallographic theory as well as basic practical experience. The theory includes Fourier transforms, crystallisation, space group determination, data collection and experimental determination of phases ( including the method of isomorphous and molecular replacement, and MAD phasing).

The interpretation of electron density maps as a 3D structure will be discussed, as well as the refinement of macromolecular structures.

The course will make use of high performance computer graphics both for the display of macromolecules and crystallographic work.

Laborative work:

Preparation of protein crystals.

Collection of diffraction data using 2D area detectors.

Solving crystallographic problems using diffraction data collected by the students and researchers at the Dep't of Molecular Biology.

Instruction

Lectures and laboratory work.

Assessment

Written exam at the end of the course. Practical exercises and laboratory work are assigned 1 point.