Schedule, syllabus and examination date

Course content

Symmetry, space groups, crystals and crystallization, diffraction, Bragg's law, Fourier synthesis and Fourier analysis, phase problem. Instrumentation, data collection and data processing. Structure determination by multiple isomorphous replacement (MIR), multiple anomalous dispersion (MAD) and molecular replacement (MR). Patterson function, Patterson maps and electron density maps. Refinement and validation. Data bases. Reading and understanding a crystallographic paper.

Learning outcome

The course will give a thorough introduction to protein structure determination by X-ray crystallography and briefly compare this method to macromolecular structure determination by electron diffraction and nuclear magnetic resonance (NMR). It is intended to enable the participants to understand and judge modern research literature in the field. The course is comprised of a theoretical part, which covers most aspects of protein crystallography, and a practical part with hands-on practicals on protein crystallization, data collection, model building and the validation of protein structures as well as simple database searches.

Admission

Students who are admitted to study programmes at UiO must each semester register which courses and exams they wish to sign up for in Studentweb.

If you are not already enrolled as a student at UiO, please see our information about admission requirements and procedures.

Prerequisites

Recommended previous knowledge

Basic knowledge of proteins and proficiency in mathematics is recommended.

Overlapping courses

The course overlaps in 9 study points with KJ-KJB324 and 10 studypoints with KJM4350

Teaching

The course comprises of 27 hours of lectures and 30 hours of compulsory theoretical exercises and discussion session, 8 hours of compulsory laboratory practicals, and a compulsory literature task that students are to present orally as well as in writing. The project task has to be approved before you can enter the final examination.

The first lecture is mandatory. If you are unable to join, you have to inform the Expedition Office in advance (phone 22 85 54 46). If not, you will loose the access to the course and to the examination.

Access to teaching

A student who has completed compulsory instruction and coursework and has had these approved, is not entitled to repeat that instruction and coursework. A student who has been admitted to a course, but who has not completed compulsory instruction and coursework or had these approved, is entitled to repeat that instruction and coursework, depending on available capacity.

Examination

Presentation of a literature task, orally and in writing. Prepared participation in theoretical exercises and discussion session. Written summary of laboratory practicals (not to exceed 2 pages/report). Oral examination. Course grades are awarded on a descending scale using alphabetic grades from A to E for passes and F for fail.

Examination support material

No examination support material is allowed.

Language of examination

You may submit your response in Norwegian, Swedish, Danish or English. If you would prefer to have the exam text in English, you may apply to the course administrators.

Explanations and appeals

Special examination arrangements

Application form, deadline and requirements for special examination arrangements.

Other

Written exercises are only valid for one semester.

The teaching will be cancelled if less than 3 students are registered for the course at the registration deadline.

Facts about this course

Credits
10
Level
Bachelor
Teaching

This version of the course was held for the last time Spring 2007. KJM4350 - Protein crystallography will still be held, but will be moved from spring to fall.

Students who would like to sign up for the exam in this version of the course should first sign up for the version which will still be held, and then contact the Department of Chemistry.

Examination
Every autumn
Teaching language
English