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The dopamine D2 long (D2L) receptor and bacteriorhodopsin (bR), which are integral membrane proteins, have been incorporated within bicontinuous cubic mesophases formed by the lipids anandamide and H-farnesoyl monoethanolamide, which have been specifically investigated by us for use as in meso crystallization media. We show that the incorporated membrane protein affects the structure of the cubic phases with the particular effect observed dependent on the geometry of the underlying cubic phase. The results are complementary to those obtained in Part 1 of this series, where we demonstrated that the structural effects observed depend on the structure of the membrane protein. Importantly protein concentrations commonly used for crystallization can destroy the cubic phase matrix, particularly where there is a large discrepancy between the hydrophilic and the hydrophobic spans of the membrane protein, and the hydrophilic and hydrophobic domain sizes of the cubic phase.
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Conn et al. (2010) studied this question.
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