The course gives an introduction to methods for structure determination of biological macromolecules with special focus on diffraction based methods.
After passing the course the student should be able to
account for basic Fourier optics theory and its applications in structure determination of biological macromolecules
account for basic concepts in X-ray crystallographic theory
account for basic methods that are used in macromolecular crystallography
build models of macromolecules by means of electron density maps and analyse the possible errors of such models by means of different validation methods
critically review and evaluate structures solved with X-ray crystallography
account for requirements, possibilities and limitations of different structure determination methods and for the information provided by the different methods.
Basics This course module covers basic concepts and theory of diffraction (both X-ray and electron diffraction) and Fourier optics and gives a basis to understand several of the most important methods for biomacromolecular structure determination (X-ray diffraction, cryo-EM). The concepts and the theory are developed, and are applied in later parts of the course.
X-Ray Crystallography Here, the theory for X-ray crystallography and its application in modern methods for structure determination of biological macromolecules is further developed. Topics covered include collection and processing of data from synchrotron radiation sources, experimental phasing, interpretation of electron density maps and modelling, refinement and validation of structural models. Students will also get practical experience of all essential stages in a structure determination. The course module gives the students the knowledge and experience needed to critically review and evaluate structures solved with X-ray crystallography.
Other methods: Cryo-EM, XFEL single particle imaging, SAXS Focus will be on cryo electron microscopy, that in recent years has progressed greatly and is rapidly becoming an attractive alternative to X-ray crystallography for structure determination of larger (>250 the kDa) biological macromolecules, but XFEL single particle imaging, SAXS, and NMR will also be introduced.
Lectures, literature seminars, laboratory sessions and computer exercises. Participation in seminars, laboratory sessions and computer exercises are compulsory.
Written examination (6 credits). Seminars, exercises and laboratory sessions (4 credits).
week 27, 2017
Biomolecular crystallography : principles, practice, and application to structural biology