| Autor: |
McIlwain BC; Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA. mcilwain@umich.edu., Kermani AA; Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA. kermania@umich.edu. |
| Jazyk: |
angličtina |
| Zdroj: |
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2020; Vol. 2127, pp. 13-27. |
| DOI: |
10.1007/978-1-0716-0373-4_2 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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