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Protein Science (2008), 17:623-632. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Analysis of solvent content and oligomeric states in protein crystals—does symmetry matter?

Maksymilian Chruszcz1, Wojciech Potrzebowski1,2, Matthew D. Zimmerman1, Marek Grabowski1, Heping Zheng1, Piotr Lasota1, and Wladek Minor1

1 Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908, USA
2 Technical University of Lodz, Institute of Physics, 90-924 Lodz, Poland

(RECEIVED November 15, 2007; FINAL REVISION January 24, 2008; ACCEPTED January 29, 2008)

A nonredundant set of 9081 protein crystal structures in the Protein Data Bank was used to examine the solvent content, the number of polypeptide chains, and the oligomeric states of proteins in crystals as a function of crystal symmetry (as classified by crystal systems and space groups). It was found that there is a correlation between solvent content and crystal symmetry. Surprisingly, proteins crystallizing in lower symmetry systems have lower solvent content compared to those crystallizing in higher symmetry systems. Nevertheless, there is no universal correlation between solvent content and preferences of macromolecules to crystallize in certain space groups. Crystal symmetry as a function of oligomeric state was examined, where trimers, tetramers, and hexamers were found to prefer to crystallize in systems where the oligomer symmetry could be incorporated in the crystal symmetry. Our analysis also shows that the frequency distribution within the enantiomorphous pairs of space groups does not differ significantly, in contrast to previous reports.

Keywords: solvent content; Matthews coefficient; protein crystals; oligomerization; space group frequency


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