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C‐phycocyanin as a highly attractive model system in protein crystallography: unique crystallization properties and packing‐diversity screening
Author(s) -
Sarrou Iosifina,
Feiler Christian G.,
Falke Sven,
Peard Nolan,
Yefanov Oleksandr,
Chapman Henry
Publication year - 2021
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798320016071
Subject(s) - crystallization , protein crystallization , crystallography , diffraction , crystal (programming language) , fluorescence , materials science , crystal structure , molecule , x ray crystallography , chemistry , computer science , physics , optics , organic chemistry , programming language
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.