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Publication Abstract from PubMed

The crystal structure of C-phycocyanin from the cyanobacterium S. platensis has been determined at 2.2 A resolution. The crystals belong to the monoclinic crystal form, which has not been previously reported for phycobiliprotein structures. The structure was solved using the molecular-replacement method with a final R value of 18.9% (R(free) = 23.7%) after model building and refinement. In the crystals used for the study, the C-phycocyanin hexamers formed by face-to-face association of two trimers are arranged in layers rather than in columns. Three different kinds of packing between adjacent hexamers in the layer were compared. The tight packing of two adjacent hexamers formed by four trimers in the asymmetric unit brings beta155 PCB chromophores close together, so it is possible that lateral energy transfer takes place through the beta155-beta155 route.

Structure of C-phycocyanin from Spirulina platensis at 2.2 A resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes.,Wang XQ, Li LN, Chang WR, Zhang JP, Gui LL, Guo BJ, Liang DC Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):784-92. Epub 2001, May 25. PMID:11375497^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.