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Updated: Feb 8, 2026
Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
Published on: December 28, 2019
The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain
Aengus Mac Sweeney1, Alain Chambovey1, Micha Wicki1
1Drug Discovery Biology, Idorsia Pharmaceuticals Ltd., Allschwil, Switzerland.
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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