Use of Escherichia coli for the Production and Purification of Membrane Proteins

Vincent G. L. Postis, Andrea E. Rawlings, Amelia Lesiuk, Stephen A. Baldwin

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Citations (Scopus)


Individual types of ion channels and other membrane proteins are typically expressed only at low levels in their native membranes, rendering their isolation by conventional purification techniques difficult. The heterologous over-expression of such proteins is therefore usually a prerequisite for their purification in amounts suitable for structural and for many functional investigations. The most straightforward expression host, suitable for prokaryote membrane proteins and some proteins from eukaryotes, is the bacterium Escherichia coli. Here we describe the use of this expression system for production of functionally active polytopic membrane proteins and methods for their purification by affinity chromatography in amounts up to tens of milligrams.
Original languageEnglish
Title of host publicationIon Channels
EditorsN. Gamper
PublisherHumana Press
Number of pages22
ISBN (Electronic)9781627033510
ISBN (Print)9781627033503
Publication statusPublished - 2013

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029


  • Membrane protein
  • Protein expression
  • Nonionic detergent
  • Protein purification
  • Affinity chromatography
  • Size exclusion chromatography


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