Elective course in MSc Life Science and Technology, MSc Chemistry.
Students with a BSc degree in LST, MST, or BSc degree in Biology/Chemistry or equivalent can enroll in this course. It is recommended to have a basic understanding of biochemistry.
To gain a deeper understanding of protein function it is important to decipher the three-dimensional structure of proteins. This structural knowledge can serve as a basis for rational drug design for therapeutic applications such as the development of novel or improved antibiotics. This course introduces the current state-of-the-art techniques in structural biology, with a focus on X-ray crystallography. The principles of X-ray crystallography will be introduced in a series of lectures alongside practical exercises in crystallization, structure determination and validation. Furthermore, state of the art structural biology methods (single-particle cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), and nuclear magnetic resonance spectroscopy (NMR)) will be introduced and compared to X-ray crystallography.
At the end of the course participants will understand the theoretical principles behind the mentioned techniques and will be able to judge which technique to use for which use-case.
Students will be graded based on a final exam and on short presentations, in which students discuss the quality of three-dimensional structures of selected scientific publications.
The students following this course will be trained to:
set up protein crystallization experiments using vapor diffusion techniques
perform crystal soaking experiments to generate heavy metal derivatives or co-crystallize small molecules
prepare crystals for X-ray measurements (vitrification of crystals)
process and analyze diffraction data
determine three-dimensional protein structures using the most common methods (Single Anomalous Dispersion, Molecular Replacement)
perform structure modelling and refinement
validate the quality of protein structures
deposit refined structures at the protein data bank
differentiate structural biology methods depending on the scientific question (X-ray crystallography ,NMR, cryo-EM, cryo-ET)
analyze and present a structural biology publication
Schedule information can be found on the website of the programmes.
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For more information, watch the video or go the the 'help-page' in MyTimetable. Please note: Joint Degree students Leiden/Delft have to merge their two different timetables into one. This video explains how to do this.
Mode of Instruction
Lecture, seminar, practical exercises
Written examination with short and essay questions (80%)
It is recommended to revisit and further explore the course content by reading “Biomolecular Crystallography – Bernhard Rupp – 1st edition – ISBN: 978-0-8153-4081-2”.
From the academic year 2022-2023 on every student has to register for courses with the new enrollment tool MyStudyMap. There are two registration periods per year: registration for the fall semester opens in July and registration for the spring semester opens in December. Please see this page for more information.
Please note that it is compulsory to both preregister and confirm your participation for every exam and retake. Not being registered for a course means that you are not allowed to participate in the final exam of the course. Confirming your exam participation is possible until ten days before the exam.
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Dr. S.R.J. Geibel, Dr. S. Brünle
According to OER article 4.8, students are entitled to view their marked examination for a period of 30 days following the publication of the results of a written examination. Students should contact the lecturer to make an appointment for such an inspection session.