Polyoxometalates: more than a phasing tool in protein crystallography View Full Text


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Article Info

DATE

2018-10

AUTHORS

Aleksandar Bijelic, Annette Rompel

ABSTRACT

Protein crystallography is the most widely used method for determining the molecular structure of proteins and obtaining structural information on protein-ligand complexes at the atomic level. As the structure determines the functions and properties of a protein, crystallography is of immense importance for nearly all research fields related to biochemistry. However, protein crystallography suffers from some major drawbacks, whereby the unpredictability of the crystallization process represents the main bottleneck. Crystallization is still more or less a 'trial and error' based procedure, and therefore, very time and resource consuming. Many strategies have been developed in the past decades to improve or enable the crystallization of proteins, whereby the use of so-called additives, which are mostly small molecules that make proteins more amenable to crystallization, is one of the most convenient and successful methods. Most of the commonly used additives are, however, restricted to particular crystallization conditions or groups of proteins. Therefore, a more universal additive addressing a wider range of proteins and being applicable to a broad spectrum of crystallization conditions would represent a significant advance in the field of protein crystallography. In recent years, polyoxometalates (POMs) emerged as a promising group of crystallization additives due to their unique structures and properties. In this regard, the tellurium-centered Anderson-Evans polyoxotungstate [TeW6O24]6- (TEW) showed its high potential as crystallization additive. In this lecture text, the development of POMs as tools in protein crystallography are discussed with a special focus on the so far most successful cluster TEW. More... »

PAGES

10

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s40828-018-0064-1

DOI

http://dx.doi.org/10.1007/s40828-018-0064-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1106366457

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30596006


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