1JBO

The 1.45A Three-Dimensional Structure of c-Phycocyanin from the Thermophylic Cyanobacterium Synechococcus elongatus

Summary for 1JBO

• Entry DOI: 10.2210/pdb1jbo/pdb
• Descriptor: C-Phycocyanin alpha chain, C-Phycocyanin beta chain, PHYCOCYANOBILIN, ... (4 entities in total)
• Functional Keywords: photosynthesis
• Biological source: Synechococcus elongatus; More
• Cellular location: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P50032 P50033
• Total number of polymer chains: 2
• Total formula weight: 37439.36

Authors

Nield, J.,Rizkallah, P.J.,Barber, J.,Chayen, N.E. (deposition date: 2002-05-02, release date: 2003-03-18, Last modification date: 2023-08-16)

Primary citation

Nield, J.,Rizkallah, P.J.,Barber, J.,Chayen, N.E.
The 1.45A three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus
J.STRUCT.BIOL., 141:149-155, 2003

PubMed 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.

PubMed: 12615541
DOI: 10.1016/S1047-8477(02)00609-3

Experimental method

X-RAY DIFFRACTION (1.45 Å)