Protein surface shielding agents in protein crystallization
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
21169691
PubMed Central
PMC3004254
DOI
10.1107/s0909049510032450
PII: S0909049510032450
Knihovny.cz E-resources
- MeSH
- X-Ray Diffraction MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Crystallization * methods MeSH
- Polyethylene Glycols chemistry MeSH
- Surface Properties MeSH
- Proteins chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Polyethylene Glycols MeSH
- Proteins MeSH
The molecules adhering temporarily on the surface of protein molecules change the propensity of protein molecules to deposit on the crystal surface in a definite position and orientation. The concepts of competitive adhesion modes and protein surface shielding agents acting on the surface of molecules in a non-equilibrium process of protein crystallization provide a useful platform for the control of crystallization. The desirable goal, i.e. a transient preference of a single dominating adhesion mode between protein molecules during crystallization, leads to uniform deposition of proteins in a crystal. This condition is the most important factor for diffraction quality and thus also for the accuracy of protein structure determination. The presented hypothesis is a generalization of the experimentally well proven behaviour of hydrophilic polymers on the surface of protein molecules of other compounds.
See more in PubMed
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