Membrane protein structural biology is critically dependent upon the supply of high-quality protein. Over the last few years, the value of crystallising biochemically characterised, recombinant targets that incorporate stabilising mutations has been established. Nonetheless, obtaining sufficient yields of many recombinant membrane proteins is still a major challenge. Solutions are now emerging based on an improved understanding of recombinant host cells; as a 'cell factory' each cell is tasked with managing limited resources to simultaneously balance its own growth demands with those imposed by an expression plasmid. This review examines emerging insights into the role of translation and protein folding in defining high-yielding recombinant membrane protein production in a range of host cells.
Bibliographical noteFunding: Biotechnology and Biological Sciences Research Council (BBSRC; grant BB/I019960/1) and the Innovative Medicines Joint Undertaking under
Grant Agreement no. 115583 to the ND4BB ENABLE Consortium. BBSRC (grant BB/I010351/1) and from the Leverhulme Trust (grant RPG-2014-032).