C8800 X-ray Structure Analysis

Faculty of Science
Spring 2007
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
there are 21 fields of study the course is directly associated with, display
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.
The course is also listed under the following terms Spring 2008 - for the purpose of the accreditation, Spring 2011 - only for the accreditation, Spring 2000, Spring 2001, Spring 2002, Spring 2003, Spring 2004, Spring 2005, Spring 2006, Spring 2008, Spring 2009, Spring 2010, Spring 2011, Spring 2012, spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2015, Spring 2016, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2023, Spring 2024, Spring 2025.
  • Enrolment Statistics (Spring 2007, recent)
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