期刊
IUCRJ
卷 4, 期 -, 页码 734-740出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252517012349
关键词
polyoxotungstate; crystallization additives; crystal contacts; liquid-liquid phase separation; solvent entropy
资金
- Austrian Science Fund (FWF) [P27534, P25217]
- Austrian Science Fund (FWF) [P 25217] Funding Source: researchfish
- Austrian Science Fund (FWF) [P25217] Funding Source: Austrian Science Fund (FWF)
The limiting factor in protein crystallography is still the production of high-quality crystals. In this regard, the authors have recently introduced hexatungstotellurate(VI) (TEW) as a new crystallization additive, which proved to be successful within the liquid-liquid phase separation (LLPS) zone. Presented here are comparative crystal structure analyses revealing that protein-TEW binding not only induces and stabilizes crystal contacts, but also exhibits a significant impact on the solvent-driven crystallization entropy, which is the driving force for the crystallization process. Upon the formation of TEW-mediated protein-protein contacts, the release of water molecules from the hydration shells of both molecules, i.e. TEWand the protein, causes a reduced solvent-accessible surface area, leading to a significant gain in solvent entropy. Based on the crystal structures of aurone synthase (in the presence and absence of TEW), insights have also been provided into the formation of a metastable LLPS, which is caused by the formation of protein clusters, representing an ideal starting point in protein crystallization. The results strongly encourage the classification of TEW as a valuable crystallization additive.
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