PřF:C8800 X-ray Structure Analysis - Course Information
C8800 X-ray Structure Analysis
Faculty of ScienceSpring 2006
- Extent and Intensity
- 2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
- Guaranteed by
- doc. RNDr. Jaromír Marek, Ph.D.
Department of Chemistry – Chemistry Section – Faculty of Science - Course Enrolment Limitations
- The course is also offered to the students of the fields other than those the course is directly associated with.
- fields of study / plans the course is directly associated with
- Analytical Chemistry (programme PřF, D-CH) (2)
- Analytical Chemistry (programme PřF, M-CH)
- Inorganic Chemistry (programme PřF, D-CH) (2)
- Inorganic Chemistry (programme PřF, M-CH)
- Inorganic Chemistry (programme PřF, N-CH)
- Biochemistry (programme PřF, M-CH)
- Physical Chemistry (programme PřF, D-CH) (2)
- Physical Chemistry (programme PřF, M-CH)
- Macromolecular Chemistry (programme PřF, D-CH) (2)
- Chemistry (programme PřF, M-CH)
- Environmental Chemistry (programme PřF, D-CH) (2)
- Environmental Chemistry (programme PřF, M-CH)
- Macromolecular Chemistry (programme PřF, M-CH)
- Organic Chemistry (programme PřF, D-CH) (2)
- Organic Chemistry (programme PřF, M-CH)
- Course objectives
- Symmetry of matter, point groups, symmetry of diffraction image, Laue classes, primitive and Bravais cell, space groups.
Diffraction of X-ray, Thompson scattering, interference of scattered waves, atomic and structure factor, Bragg and Laue equations, Ewald sphere, intensity of diffracted X-ray, Fourier synthesis
Diffraction experiment, sources of X-ray, synchrotrons, detectors, diffractometers, cryocrystallography. Indexation, integral intensity, reduction, Lorenz, polarisation and absorption correction
Phase problem, Patterson function and method, probability distribution of structure factors, direct methods, R-factors, least-square-method, SHELXS a SHELXL.
Crystallisation of macromolecules, methods of sitting and hanging drop, seeding. Phase problems and proteins, molecular replacements, methods of heavy atom derivatives, (SIR, MIR, MIRAS), MAD and selenoproteins selenoproteins. Maps of electron density. Fourier transformations. Building of the model and model refinement. Least-square-method, constrains, restrains. Protein. crystallography in post-genomic era
Crystallographic databases. - Syllabus
- Symmetry of matter
- Interaction of X-ray with matter
- Diffraction by crystal
- Sources and detectors of X-ray
- Diffractometer
- Phase problem
- Patterson and direct methods
- Refinement, R-factors, Least-square-method
- Programs SHELXS and SHELXL.
- Crystallisation of protein crystals
- Methods of heavy derivatives of proteins
- Refinement of protein structures
- Crystallographic databases.
- Literature
- MAREK, Jaromír and Z. TRÁVNÍČEK. Monokrystalová rentgenová strukturní analýza (Single crystal X-ray structure analysis). první. Olomouc: Vydavatelství Univerzity Palackého, 2002, 169 pp. nedělí se na edice. ISBN 80-244-0551-2. info
- GIACOVAZZO, C. Fundamentals of Crystallography. 1992. ISBN 0-19-855578-4. info
- Assessment methods (in Czech)
- ústní zkouška či kolokvium
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
The course is taught: every week.
- Enrolment Statistics (Spring 2006, recent)
- Permalink: https://is.muni.cz/course/sci/spring2006/C8800