Abstract
Metal-chelating iminodiacetate (IDA) lipid monolayers at the air/water interface have been engineered to promote the 2D crystallization of proteins which display solvent-accessible histidines. The physical properties of IDA lipid monolayers have been specifically tailored to allow the binding and 2D assembly of added proteins. Fluorescently labeled IDA lipid monolayers allow us to monitor the formation of the protein crystals optically. Here we review our efforts in the interfacial crystallization of streptavidin as monitored using fluorescence, Brewster angle and transmission electron microscopy and discuss future challenges in this area.
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