The 1.45 Å 3D structure of C-phycocyanin from Synechococcus elongatus
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The 1.45 Å 3D structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus |
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| - adapted from: Jon Nield, Pierre Rizkallah, James Barber & Naomi Chayen. J. Struct. Biol.: 141:149-155 | |
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| 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 di.erent types of organisms. We report here the 1.45 Angstrom resolution three-dimensional structure of one such pigment protein, C-phycocyanin, from Synechococcus elongatus, Kovrov strain. The structure is at the highest resolution achieved for any such phycobiliprotein to date. 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 7 h under nucleation conditions and then transferring them to metastable conditions for growth. This is done without touching the crystallization drops throughout the process. © 2003 Elsevier Science (USA). All rights reserved. doi:10.1016/S1047-8477(02)00609-3. | |
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CONTENTS
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| Straight to Introduction | |
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© Journal of Structural Biology, 2003