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The production of recombinant integral membrane proteins for structural and functional studies remains technically challenging due to their relatively low levels of expression. To address this problem, screening strategies have been developed to identify the optimal membrane sequence and expression host for protein production. A common approach is to genetically fuse the membrane protein to a fluorescent reporter, typically Green Fluorescent Protein (GFP) enabling expression levels, localization and detergent solubilisation to be assessed. Initially developed for screening the heterologous expression of bacterial membrane proteins in Escherichia coli, the method has been extended to eukaryotic hosts, including insect and mammalian cells. Overall, GFP-based expression screening has made a major impact on the number of membrane protein structures that have been determined in the last few years.

Original publication




Journal article


Adv Exp Med Biol

Publication Date





1 - 11


Escherichia coli, Green fluorescent protein, HEK 293 cells, Insect cells, Integral membrane protein, Pichia pastoris, Saccharomyces cerevisiae, Animals, Cells, Cultured, Escherichia coli, Eukaryotic Cells, Gene Expression, Genes, Reporter, Green Fluorescent Proteins, HEK293 Cells, Humans, Insecta, Luminescent Proteins, Membrane Proteins, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Yeasts