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

Sarrou, I.; Feiler, C.G.; Falke, S.; Peard, N.; Yefanov, O.; Chapman, H.

doi:10.1107/S2059798320016071

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 4
Crystal packing and structural details of C-PC crystallized in the rhombohedral space group R32 (data set 10, Supplementary Table S3). (a) The unit-cell content is depicted as an overlay in the crystal-packing context. (b) B-factor plot as a function of position in the individual heterodimeric C-PC molecules. (c) Each heterodimeric C-PC molecule harbours three attached phycocyanobilin ligands (yellow). (d) The dodecameric ring structure with the top ring in cartoon representation and the bottom ring as a surface (grey).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 77| Part 2| February 2021| Pages 224-236

https://doi.org/10.1107/S2059798320016071

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