C-phycocyanin as a highly attractive model system in protein crystallography: unique crystallization properties and packing-diversity screening

Autor:	Henry N. Chapman, Sven Falke, Oleksandr Yefanov, Iosifina Sarrou, Christian G. Feiler, Nolan Peard
Rok vydání:	2021
Předmět:	Models Molecular Diffraction Materials science Protein Conformation Neutron diffraction Thermosynechococcus Life Sciences Building Blocks of Life Structure and Function Model system C-Phycocyanin Crystallography X-Ray law.invention Crystal Bacterial Proteins Structural Biology law ddc:530 precipitant Crystallization Phycocyanin C-phycocyanin Research Papers Fluorescence Crystallography X-ray crystallography crystallization determinants model system crystal packing
Zdroj:	Acta crystallographica / Section D 77(2), 224-236 (2021). doi:10.1107/S2059798320016071 Acta Crystallographica. Section D, Structural Biology
ISSN:	2059-7983
Popis:	Acta crystallographica / Section D 77(2), 224 - 236 (2021). doi:10.1107/S2059798320016071 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. Published by Wiley, Bognor Regis
Databáze:	OpenAIRE
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