Course or Conference 4: Difference between revisions

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The goal of the course is to present methods of macromolecular crystallization and give hands-on experience with them.  Participants may bring their own proteins. The course is divided into 50% lectures and 50% laboratory sessions.  Limit: 20 participants.
*Topics to be covered by lectures and laboratory sessions include:
*Conventional techniques and their modifications.
*High-throughput crystallization screening.
*The path to crystals.  The phase diagram and the kinetics of equilibration.
*Optimization: Exploiting protein formulation, cocktail formulation, and time to equilibration.
*Using a microfluidic device to determine protein precipitation boundaries.
*A pro-active strategy for crystallization.
*Oils as tools for crystallization.
*How to choose your method of crystallization.
*Seeding as an optimization tool.
*Interpretation of the crystallization drop phenomenon:  recognizing what you see.
*Does it matter what screen that you use?
*Biophysical tools for crystallization:  mass spectroscopy, dynamic light scattering, Thermofluor.
*Crystal clear communication: the role of LIMS in a crystallization laboratory.
*Cryoprotection.


[[http://xray.bmc.uu.se/~terese/course/course.htm Official course page]]

Latest revision as of 17:08, 18 October 2008

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