title: Crystallizing transmembrane peptides in lipidic mesophases.
abstract: Structure determination of membrane proteins by crystallographic means has been facilitated by crystallization in lipidic mesophases. It has been suggested, however, that this so-called in meso method, as originally implemented, would not apply to small protein targets having </=4 transmembrane crossings. In our study, the hypothesis that the inherent flexibility of the mesophase would enable crystallogenesis of small proteins was tested using a transmembrane pentadecapeptide, linear gramicidin, which produced structure-grade crystals. This result suggests that the in meso method should be considered as a viable means for high-resolution structure determination of integral membrane peptides, many of which are predicted to be coded for in the human genome.
authors.affiliation: Membrane Structural and Functional Biology Group, School of Biochemistry and Immunology, and School of Medicine, Trinity College, Dublin, Ireland.
authors.forename: Nicole
authors.initials: N
authors.lastname: Höfer
authors.forename: David
authors.initials: D
authors.lastname: Aragão
authors.forename: Martin
authors.initials: M
authors.lastname: Caffrey
mesh_terms: D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D006096:Gramicidin / Q000737:chemistry; D006801:Humans; D008563:Membrane Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D044367:Phase Transition
chemical_list: D008563:Membrane Lipids; D008565:Membrane Proteins; D010455:Peptides; D006096:Gramicidin