Memb-PASS™ Membrane Protein Crystallography

Use less protein and accelerate the process of crystallizing membrane proteins using the new patent-pending Memb-PASS™ (Prompt Assay of Size and Stability) technology, developed by Dr. Michael Wiener and members of his laboratory at the University of Virginia.

Memb-PASS™ starts with a Differential Filtration Detergent Assay, a microplate-based detergent screening method that rapidly characterizes the stability and size of membrane proteins exchanged into a ninety-four detergent panel provided with the Memb-PASS™ Differential Filtration Detergent Assay. The entire assay utilizes sub-milligram quantities of membrane protein, and requires only several hours to perform while quickly helping you select the best detergent complex for your membrane protein! [1] After the protein is in a suitable detergent, as determined by the Memb-PASS™ Differential Filtration Assay, the Memb-PASS™ Solubility Screen, with twenty-four conditions, is applied to determine the proper protein concentration for crystallization. Once at proper concentration, the membrane protein can then be set up for crystallization with the Memb-PASS™ Crystallization Screen, an innovative, ninety-six condition screen, developed for integral membrane protein crystallization based on conditions that resulted in successful crystallization of membrane proteins.

The Memb-PASS™ methods are specifically designed to work together to help you significantly reduce the amount of protein, reagents and time spent on the crystallization of membrane proteins.

Available Products

• Memb-PASS™ Differential Filtration Detergent Assay
• Memb-PASS™ High and Low MWCO Filtration Plates
• Memb-PASS™ Solubility Screen
• Memb-PASS™ Crystallization Screen


 

Flyer Memb-PASS^TM (PDF, 1.1 MB)

 

References

[1] Vergis et al. (2010) A high-throughput differential filtration assay to screen and select detergents for membrane proteins. Anal. Biochem. 407:1.
[2] Vergis et al. (2011) The variable detergent sensitivity of proteases that are utilized for recombinant protein affinity tag removal. Prot. Expr. Purif. 78:139.