Expression in Escherichia coli: becoming faster and more complex

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


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Analytic Sample Preparation Methods
  • Escherichia coli / metabolism*
  • High-Throughput Screening Assays
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics


  • Recombinant Proteins