The Anderson-Evans Polyoxotungstate [TeW6O24]6- (TEW) is a universal and flexible crystallization additive that is integrated in our XP Screens. It was shown to improve crystal quality and resolution by:
Figure 2 (right): Chemical structure of TEW. Figure from .
The XP Screen is a convenient initial screen that has successfully induced protein crystallization with low TEW concentrations such as 1 mM[5,6]. In some cases however, higher concentration of 5 or 10 mM TEW are needed.
The XP Up Screen is an upgrade of the well-established XP Screen. It contains 96 of the most prominent screening solutions that are long-term stable in the presence of up to 10 mM TEW.
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 Bijelic et al. (2017) Ten Good Reasons for the Use of the Tellurium-Centered Anderson-Evans Polyoxotungstate in Protein Crystallography. Acc. Chem. Res. 50:1441.
 Molitor et al. (2016) In situ formation of the first proteinogenically functionalized [TeW6O24O2(Glu)]7- structure reveals unprecedented chemical and geometrical features of the Anderson-type cluster. Chem. Commun. 52:12286.
 Bijelic et al. (2015) Hen Egg-White Lysozyme Crystallisation: Protein Stacking and Structure Stability Enhanced by a Tellurium(VI)-Centred Polyoxotungstate. ChemBioChem 16:233.
 Mauracher et al. (2014) Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal. Acta Cryst. D 70:2301.
 Sobala et al. (2020) Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target. PNAS 117 (47):29595.
 Ames et al. (2020) Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins. Front. Microbiol. 11:959.
 Mac Sweeney et al. (2018) The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms. PLOS one 13 (6): e0199639.