ArticlePloS one2018
The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- Speciation atlas of polyoxometalates in aqueous solutions.Science advances · 2023Article
- Protein Frameworks with Thiacalixarene and Zinc.Crystal growth & design · 2022Article
- Conformational flexibility in the zinc solute-binding protein ZnuA.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Speciation of Transition-Metal-Substituted Keggin-Type Silicotungstates Affected by the Co-crystallization Conditions with Proteinase K.Inorganic chemistry · 2021Article
- Wells-Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study.Scientific reports · 2021Article
- Selective Modulation of Dynamic Protein Complexes.Cell chemical biology · 2020Review
- Protein crystal structure determination with the crystallophore, a nucleating and phasing agent.Journal of applied crystallography · 2019Article
- Article
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Abstract
The use of the tellurium-centered Anderson-Evans polyoxotungstate [TeW6O24]6- (TEW) as a crystallization additive has been described. Here, we present the use of TEW as an additive in the crystallization screening of the nucleotide binding domain (NBD) of HSP70. Crystallization screening of the HSP70 NBD in the absence of TEW using a standard commercial screen resulted in a single crystal form. An identical crystallization screen of the HSP70 NBD in the presence of TEW resulted in both the "TEW free" crystal form and an additional crystal form with a different crystal packing. TEW binding was observed in both crystal forms, either as a well-defined molecule or in overlapping alternate positions suggesting translational disorder. The structures were solved by both molecular replacement and single wavelength anomalous diffraction (SAD) using the anomalous signal of a single bound molecule of TEW. This study adds one more example of TEW binding to a protein and influencing its crystallization behavior.
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