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Analysis of solvent content and oligomeric states in protein crystals—does symmetry matter?
Author(s) -
Chruszcz Maksymilian,
Potrzebowski Wojciech,
Zimmerman Matthew D.,
Grabowski Marek,
Zheng Heping,
Lasota Piotr,
Minor Wladek
Publication year - 2008
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.073360508
Subject(s) - solvent , crystallography , crystal (programming language) , symmetry (geometry) , chemistry , macromolecule , oligomer , crystallographic point group , crystal structure , space group , protein crystallization , symmetry operation , chemical physics , crystallization , physics , x ray crystallography , mathematics , quantum mechanics , organic chemistry , diffraction , biochemistry , geometry , computer science , programming language
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.