title: Advances and challenges of membrane-protein complex production.
abstract: Most membrane-proteins exist in complexes rather than isolated entities. To fully understand their biological function it is essential to study the intact membrane-protein assemblies. The overexpression and purification of many essential membrane-protein complexes is still a considerable and often unsurmountable challenge. In these cases, extraction from source is the only option for many large multi-subunit cellular machines. Here, we describe recent advances in overexpression of multi-subunit membrane-protein complexes, the strategies to stabilize these complexes and highlight major achievements in membrane-protein structural research that were facilitated by the prospect of achieving subnanometer to near-atomic resolution by electron cryo-microscopy.
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, Grenoble 38042, France; Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, Grenoble 38042 France.
authors.forename: Sarah
authors.initials: S
authors.lastname: Zorman
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, Grenoble 38042, France; Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, Grenoble 38042 France.
authors.forename: Mathieu
authors.initials: M
authors.lastname: Botte
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, Grenoble 38042, France; Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, Grenoble 38042 France.
authors.forename: Qiyang
authors.initials: Q
authors.lastname: Jiang
authors.affiliation: School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom. Electronic address: Ian.Collinson@bristol.ac.uk.
authors.forename: Ian
authors.initials: I
authors.lastname: Collinson
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, Grenoble 38042, France; Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, Grenoble 38042 France; School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom. Electronic address: schaffitzel@embl.fr.
authors.forename: Christiane
authors.initials: C
authors.lastname: Schaffitzel
mesh_terms: D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D003001:Cloning, Molecular / Q000379:methods*; D020285:Cryoelectron Microscopy / Q000379:methods; D003902:Detergents / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D005079:Excipients / Q000737:chemistry; D006801:Humans; D007313:Insecta / Q000235:genetics; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics* / Q000648:ultrastructure; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000648:ultrastructure
chemical_list: D003902:Detergents; D005079:Excipients; D008565:Membrane Proteins; D011994:Recombinant Proteins