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Publication Abstract from PubMed

The unique crystallization properties of the antenna protein C-phycocyanin (C-PC) from the thermophilic cyanobacterium Thermosynechococcus elongatus are reported and discussed. C-PC crystallizes in hundreds of significantly different conditions within a broad pH range and in the presence of a wide variety of precipitants and additives. Remarkably, the crystal dimensions vary from a few micrometres, as used in serial crystallography, to several hundred micrometres, with a very diverse crystal morphology. More than 100 unique single-crystal X-ray diffraction data sets were collected from randomly selected crystals and analysed. The addition of small-molecule additives revealed three new crystal packings of C-PC, which are discussed in detail. The high propensity of this protein to crystallize, combined with its natural blue colour and its fluorescence characteristics, make it an excellent candidate as a superior and highly adaptable model system in crystallography. C-PC can be used in technical and methods development approaches for X-ray and neutron diffraction techniques, and as a system for comprehending the fundamental principles of protein crystallography.

C-phycocyanin as a highly attractive model system in protein crystallography: unique crystallization properties and packing-diversity screening.,Sarrou I, Feiler CG, Falke S, Peard N, Yefanov O, Chapman H Acta Crystallogr D Struct Biol. 2021 Feb 1;77(Pt 2):224-236. doi: , 10.1107/S2059798320016071. Epub 2021 Jan 26. PMID:33559611^[1]

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