| Literature DB >> 32112312 |
Benjamin C McIlwain1, Ali A Kermani2.
Abstract
Escherichia coli is the workhorse of the structural biology lab. In addition to routine cloning and molecular biology, E. coli can be used as a factory for the production of recombinant membrane proteins. Purification of homogeneous samples of membrane protein expressed in E. coli is a significant bottleneck for researchers, and the protocol we present here for the overexpression and purification of membrane proteins in E. coli will provide a solid basis to develop lab- and protein-specific protocols for your membrane protein of interest. We additionally provide extensive notes on the purification process, as well as the theory surrounding principles of purification.Entities:
Keywords: Crystallography; E. coli; Ion channel; Membrane protein; Transporter.
Mesh:
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Year: 2020 PMID: 32112312 DOI: 10.1007/978-1-0716-0373-4_2
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745