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Curr Opin Struct Biol. 2013 Jun;23(3):326-34. doi: 10.1016/j.sbi.2013.01.006. Epub 2013 Feb 17.

Expression in Escherichia coli: becoming faster and more complex.

Author information

1
Architecture et Fonction des Macromolécules Biologiques, UMR7257 CNRS, Université Aix-Marseille, Case 932, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France.

Abstract

Escherichia coli is the major expression host for the production of homogeneous protein samples for structural studies. The introduction of high-throughput technologies in the last decade has further revitalized E. coli expression, with rapid assessment of different expression strategies and successful production of an ever-increasing number of proteins. In addition, miniaturization of biophysical characterizations should soon help choosing expression strategies based on quantitative and qualitative observations. Since many proteins form larger assemblies in vivo, dedicated co-expression systems for E. coli are now addressing the reconstitution of protein complexes. Yet, co-expression approaches show an increasing experimental combinatorial intricacy when considering larger complexes. The current combination of high-throughput and co-expression technologies paves the way, however, for tackling larger and more complex macromolecular assemblies.

PMID:
23422067
DOI:
10.1016/j.sbi.2013.01.006
[Indexed for MEDLINE]

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