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Packing bridges in protein crystal structures
Author(s) -
Carugo Oliviero,
DjinovićCarugo Kristina
Publication year - 2014
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s160057671302880x
Subject(s) - crystallization , protein crystallization , nucleation , molecule , macromolecule , crystallography , chemistry , nucleic acid , small molecule , chemical physics , organic chemistry , biochemistry
On the basis of a statistical analysis of the data deposited in the Protein Data Bank [Berman et al. (2000). Nucleic Acids Res. 28 , 235–242; Bernstein et al. (1977). J. Mol. Biol. 112 , 535–542], it is shown that two symmetry‐related protein molecules are frequently bridged by a small molecule/monoatomic ion, which was used in the crystallization medium despite the fact that it is not a physiological ligand of the macromolecule. It is therefore sensible to suppose that some of the solutes used in crystallizations can favour the nucleation process by bridging and opportunely orienting adjacent protein molecules. This would explain why small changes in the composition of the crystallization solution, for example, the presence of a minor amount of a specific additive, can have a dramatic impact on the outcome of a crystallization experiment.