The functional units within cells are often macromolecular complexes rather than single species. Production of these complexes as assembled homogenous samples is a prerequisite for their biophysical and structural characterization and hence an understanding of their function in molecular terms. Co-expression in Escherichia coli has been used routinely to decipher the subunit composition, assembly, and production of whole protein complexes. Such complexes can then be used to reconstitute protein/nucleic acid complexes in vitro. In this chapter we present protocols for the widely utilized ACEMBL and pET-MCN/ pET-MCP vector series which enable the rapid and automated co-expression of protein complexes in Escherichia coli.
CITATION STYLE
Haffke, M., Marek, M., Pelosse, M., Diebold, M. L., Schlattner, U., Berger, I., & Romier, C. (2014). Characterization and production of protein complexes by co-expression in Escherichia coli. In Structural Proteomics: High-Throughput Methods: Second Edition (pp. 63–89). Springer New York. https://doi.org/10.1007/978-1-4939-2230-7_4
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