Memb-PASS Solubility Screen™

  Membrane Protein Crystallography


* Determine the Proper Protein Concentration for Crystallization

Use less protein and accelerate the process of crystallizing Membrane Proteins using the patent-pending Memb-PASS Screening Method and Kits from Omscientia by significantly reducing the number of crystallization experiments necessary to obtain crystals of membrane proteins suitable for X-ray diffraction experiments.  The Memb-PASS Solubility Screen™ and Memb-PASS Crystallization Screen are specifically designed to work together with the Memb-PASS Differential Filtration Detergent Assay.  After the protein is in a suitable detergent, as determined by the Memb-PASS Differential Filtration Detergent Assay, the Memb-PASS Solubility Screen, with 24-conditions, is used to determine the proper protein concentration for crystallization.  Once at proper concentration, the protein can then be set up for crystallization with the Memb-PASS Crystallization screen, developed and tuned for integral membrane protein crystallization.  The solubility pre-screen is extremely useful as a follow-up to the Differential Filtration Detergent Assay, because the appropriate concentration of the protein for crystallization may be very different in different "good" detergents identified with the detergent screen. 
Patent Pending

*  Quickly ascertain suitable concentration for your target protein
*  Tuned for Integral Membrane Protein Crystallization
*  Memb-PASS system is designed to work together yielding optimal results and eliminating
      the guess work of solubility and crystallization screening
*  Memb-PASS Crystallization Screen reduces the number of crystallization experiments necessary
      to obtain diffraction quality crystals of membrane proteins

Memb-PASS Step-by-Step Method Diagrams

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  Download Solubility Screen Conditions

References
Vergis JM, Purdy MD, Wiener MC. (2010 Dec 1) A high-throughput differential filtration assay to screen and select detergents for membrane proteins. Anal. Biochem. Dec 2010.  407(1):1-11.  Epub 2010 Jul 25.