title: The nanoscience behind the art of in-meso crystallization of membrane proteins.
abstract: The structural changes occurring at the nanoscale level within the lipid bilayer and driving the in-meso formation of large well-diffracting membrane protein crystals have been uniquely characterized for a model membrane protein, intimin. Importantly, the order to order transitions taking place within the bilayer and the lipidic nanostructures required for crystal growth have been shown to be general, occurring for both the cubic and the sponge mesophase crystallization pathways. For the first time, a transient fluid lamellar phase has been observed and unambiguously assigned for both crystallization pathways, present at the earliest stages of protein crystallogenesis but no longer observed once the crystals surpass the size of the average lyotropic liquid crystalline domain. The reported time-resolved structural investigation provides a significantly improved and general understanding of the nanostructural changes taking place within the mesophase during in-meso crystallization which is a fundamental advance in the enabling area of membrane protein structural biology.
authors.affiliation: RMIT University, School of Science, College of Science Engineering and Health 124 La Trobe Street, Melbourne, Victoria 3000, Australia. calum.drummond@rmit.edu.au and Biomedical Manufacturing Program, Commonwealth Scientific and Industrial Research Organisation (CSIRO), 343 Royal Parade, Parkville, Victoria 3052, Australia.
authors.forename: Alexandru
authors.initials: A
authors.lastname: Zabara
authors.affiliation: School of Chemistry, Bio21 Institute, The University of Melbourne, Melbourne, Victoria 3010, Australia.
authors.forename: Thomas G
authors.initials: TG
authors.lastname: Meikle
authors.affiliation: Biomedical Manufacturing Program, Commonwealth Scientific and Industrial Research Organisation (CSIRO), 343 Royal Parade, Parkville, Victoria 3052, Australia.
authors.forename: Janet
authors.initials: J
authors.lastname: Newman
authors.affiliation: Biomedical Manufacturing Program, Commonwealth Scientific and Industrial Research Organisation (CSIRO), 343 Royal Parade, Parkville, Victoria 3052, Australia.
authors.forename: Thomas S
authors.identifier: http://orcid.org/0000-0002-6488-0831
authors.initials: TS
authors.lastname: Peat
authors.affiliation: RMIT University, School of Science, College of Science Engineering and Health 124 La Trobe Street, Melbourne, Victoria 3000, Australia. calum.drummond@rmit.edu.au.
authors.forename: Charlotte E
authors.initials: CE
authors.lastname: Conn
authors.affiliation: RMIT University, School of Science, College of Science Engineering and Health 124 La Trobe Street, Melbourne, Victoria 3000, Australia. calum.drummond@rmit.edu.au.
authors.forename: Calum J
authors.identifier: http://orcid.org/0000-0001-7340-8611
authors.initials: CJ
authors.lastname: Drummond
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry; D003460:Crystallization; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry*; D008055:Lipids; D050866:Liquid Crystals; D008565:Membrane Proteins / Q000737:chemistry*
chemical_list: D018829:Adhesins, Bacterial; D029968:Escherichia coli Proteins; D008051:Lipid Bilayers; D008055:Lipids; D008565:Membrane Proteins; C073819:eaeA protein, E coli