title: The 1.45 A three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus.
abstract: The conversion of solar radiation to chemical energy by photosynthetic organisms provides the primary driving force for life on earth. Light energy is captured by a variety of pigments, usually bound to proteins, which vary with different types of organisms. We report here the 1.45 A resolution three-dimensional structure of one such pigment protein, C-phycocyanin, from Synechococcus elongatus. The structure is at the highest resolution achieved for any such phycobiliprotein. This level of resolution was made possible by implementing a novel crystallization method whereby nucleation is decoupled from subsequent growth, by incubating crystallizing drops for 7h under nucleation conditions and then transferring them to metastable conditions for growth. This is done without touching the crystallization drops throughout the process.
authors.affiliation: Wolfson Laboratories, Department of Biological Sciences, Imperial College London SW7 2AZ, UK.
authors.forename: Jon
authors.initials: J
authors.lastname: Nield
authors.forename: Pierre J
authors.initials: PJ
authors.lastname: Rizkallah
authors.forename: James
authors.initials: J
authors.lastname: Barber
authors.forename: Naomi E
authors.initials: NE
authors.lastname: Chayen
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D000458:Cyanobacteria / Q000648:ultrastructure*; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D008027:Light; D008958:Models, Molecular; D010798:Phycocyanin / Q000648:ultrastructure*; D013997:Time Factors
chemical_list: D010798:Phycocyanin