Membrane Protein Structural Biology Consortium:


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

Membrane Protein Structural Biology Consortium

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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Determination and application of empirically derived detergent phase boundaries to effectively crystallize membrane proteins

Membrane Protein Structural Biology Consortium

We have carried out dye-based detergent phase partitioning studies using different combinations of 10 polyethylene glycols (PEG), 11 salts, and 11 detergents to generate a significant amount of chemically diverse phase boundary data. The resulting curves were used to guide the formulation of a 1536-cocktail crystallization screen for membrane proteins. The experimentally derived phase boundary data and the 1536 membrane screen are available through the high-throughput crystallization facility located at the Hauptman-Woodward Institute.

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Variable detergent sensitivity of proteases used for recombinant protein affinity tag removal

Membrane Protein Structural Biology Consortium

Using of a panel of 94 individual detergents, the detergent sensitivity of six commonly-used proteases (enterokinase, factor Xa, human rhinovirus 3C protease, SUMOstar, tobacco etch virus protease, and thrombin) were determined.

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