Preparation of Escherichia coli cell extract for highly productive cell-free protein expression

J Struct Funct Genomics. 2004;5(1-2):63-8. doi: 10.1023/B:JSFG.0000029204.57846.7d.

Abstract

As structural genomics and proteomics research has become popular, the importance of cell-free protein synthesis systems has been realized for high-throughput expression. Our group has established a high-throughput pipeline for protein sample preparation for structural genomics and proteomics by using cell-free protein synthesis. Among the many procedures for cell-free protein synthesis, the preparation of the cell extract is a crucial step to establish a highly efficient and reproducible workflow. In this article, we describe a detailed protocol for E. coli cell extract preparation for cell-free protein synthesis, which we have developed and routinely use. The cell extract prepared according to this protocol is used for many of our cell-free synthesis applications, including high-throughput protein expression using PCR-amplified templates and large-scale protein production for structure determinations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Fractionation / methods
  • DNA, Recombinant / genetics
  • DNA, Recombinant / isolation & purification
  • DNA-Directed RNA Polymerases
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Gene Expression
  • Genomics
  • Magnetic Resonance Spectroscopy
  • Polymerase Chain Reaction
  • Proteomics
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / genetics*
  • Viral Proteins

Substances

  • DNA, Recombinant
  • Recombinant Proteins
  • Viral Proteins
  • bacteriophage T7 RNA polymerase
  • DNA-Directed RNA Polymerases