Abstract
Membrane protein structures are being determined at an ever-accelerating rate, reflecting parallel increases in both our understanding of how to generate well-diffracting crystals and the amount of resources worldwide dedicated to membrane protein structural biology. Stability of detergent-solubilized membrane proteins has long been recognized as a prime factor in dictating the probability of crystallizing any given membrane protein (1) and has underpinned many of the advances made recently. For example, this was the basis for the development of a facile screening system for the rapid identification of stable membrane proteins by fusing targets to GFP and screening the unpurified detergent-solubilized membrane proteins by fluorescence-detection size exclusion chromatography (FSEC) (2).
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