High-throughput expression and purification of membrane proteins

Filippo Mancia, James Love

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

High-throughput (HT) methodologies have had a tremendous impact on structural biology of soluble proteins. High-resolution structure determination relies on the ability of the macromolecule to form ordered crystals that diffract X-rays. While crystallization remains somewhat empirical, for a given protein, success is proportional to the number of conditions screened and to the number of variants trialed. HT techniques have greatly increased the number of targets that can be trialed and the rate at which these can be produced. In terms of number of structures solved, membrane proteins appear to be lagging many years behind their soluble counterparts. Likewise, HT methodologies for production and characterization of these hydrophobic macromolecules are only now emerging. Presented here is an HT platform designed exclusively for membrane proteins that has processed over 5000 targets.

Original languageEnglish (US)
Pages (from-to)85-93
Number of pages9
JournalJournal of Structural Biology
Volume172
Issue number1
DOIs
StatePublished - Oct 2010
Externally publishedYes

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Membrane Proteins
Crystallization
Proteins
X-Rays

Keywords

  • Detergent
  • Expression
  • High-throughput
  • Membrane proteins
  • Structural genomics
  • Structure

ASJC Scopus subject areas

  • Structural Biology

Cite this

High-throughput expression and purification of membrane proteins. / Mancia, Filippo; Love, James.

In: Journal of Structural Biology, Vol. 172, No. 1, 10.2010, p. 85-93.

Research output: Contribution to journalArticle

Mancia, Filippo ; Love, James. / High-throughput expression and purification of membrane proteins. In: Journal of Structural Biology. 2010 ; Vol. 172, No. 1. pp. 85-93.
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