CB070 Protein crystallography

Faculty of Science
Autumn 2007 - for the purpose of the accreditation
Extent and Intensity
1/0/0. 1 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
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.
Molecular replacement (MR).
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, CNS and CCP4.
  • Crystallisation of protein crystals
  • Methods of heavy derivatives of proteins
  • Molecular replacement
  • 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
Language of instruction
Czech
Further Comments
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
Listed among pre-requisites of other courses
The course is also listed under the following terms Autumn 1999, Autumn 2010 - only for the accreditation, Autumn 2000, Autumn 2001, Autumn 2002, Autumn 2003, Autumn 2004, Autumn 2005, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, autumn 2017, Autumn 2018, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023, Autumn 2024.