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Anal Biochem. 2010 Dec 1;407(1):1-11. doi: 10.1016/j.ab.2010.07.019. Epub 2010 Jul 25.

A high-throughput differential filtration assay to screen and select detergents for membrane proteins.

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Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.


Structural studies on integral membrane proteins are routinely performed on protein-detergent complexes (PDCs) consisting of purified protein solubilized in a particular detergent. Of all the membrane protein crystal structures solved to date, a subset of only four detergents has been used in more than half of these structures. Unfortunately, many membrane proteins are not well behaved in these four detergents and/or fail to yield well-diffracting crystals. Identification of detergents that maintain the solubility and stability of a membrane protein is a critical step and can be a lengthy and "protein-expensive" process. We have developed an assay that characterizes the stability and size of membrane proteins exchanged into a panel of 94 commercially available and chemically diverse detergents. This differential filtration assay (DFA), using a set of filtered microplates, requires sub-milligram quantities of purified protein and small quantities of detergents and other reagents and is performed in its entirety in several hours.

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