Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

The fine art of integral membrane protein crystallization


Thielmann,  Yvonne
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Birch, J., Axford, D., Foadi, J., Meyer, A., Eckhardt, A., Thielmann, Y., et al. (2018). The fine art of integral membrane protein crystallization. Methods, 147, 150-162. doi:10.1016/j.ymeth.2018.05.014.

Cite as: https://hdl.handle.net/21.11116/0000-0002-68B0-2
Integral membrane proteins are among the most fascinating and important biomolecules as they play a vital role in many biological functions. Knowledge of their atomic structures is fundamental to the understanding of their biochemical function and key in many drug discovery programs. However, over the years, structure determination of integral membrane proteins has proven to be far from trivial, hence they are underrepresented in the protein data bank. Low expression levels, insolubility and instability are just a few of the many hurdles one faces when studying these proteins. X-ray crystallography has been the most used method to determine atomic structures of membrane proteins. However, the production of high quality membrane protein crystals is always very challenging, often seen more as art than a rational experiment. Here we review valuable approaches, methods and techniques to successful membrane protein crystallisation.