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The fine art of integral membrane protein crystallisation

DOI: 10.1016/j.ymeth.2018.05.014 DOI Help

Authors: James Birch (Diamond Light Source; Research Complex at Harwell) , Danny Axford (Diamond Light Source) , James Foadi (Diamond Light Source) , Arne Meyer (University of Bath) , Annette Eckardt (XtalConcepts GmbH) , Yvonne Thielmann (Max Planck Institute of Biophysics) , Isabel Moraes (Research Complex at Harwell; Diamond Light Source; National Physical Laboratory)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Methods

State: Published (Approved)
Published: May 2018

Abstract: 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.

Subject Areas: Technique Development, Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
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