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XP Screen: The Protein Crystal Glue


XP Screen: The protein crystal glue

Figure adapted from [1], used by courtesy of Prof. Annette Rompel, University of Vienna, Austria


    The Anderson−Evans polyoxotungstate [TeW6O24]6− (TEW) is a universal and flexible additive for protein crystallization. With its planar structure and a central tellurium atom, it is able to stabilize flexible regions in proteins and provides an anomalous signal for phasing[1].

    TEW was shown to:

    • covalently bind and structurally adapt to fit into protein molecules (cgAUS1, PDB code: 4Z12, 4Z13)[2]
    • act as linker in various orientations and thereby create either smaller (abPPO4, PDB code: 4OUA) or larger (lysozyme, PDB code: 4PHI) protein-protein distances[3,4]
    • induce heterogeneous crystallization of two different protein forms in one single crystal (abPPO4, PDB code: 4OUA)[4]

    Our new XP Screen contains TEW in 96 of the most prominent crystallization conditions, providing an environment for TEW to improve crystallization and crystal diffraction quality especially for challenging targets.


    References:
    [1] 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.
    [2] 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.
    [3] Bijelic et al. (2015) Hen Egg-White Lysozyme Crystallisation: Protein Stacking and Structure Stability Enhanced by a Tellurium(VI)-Centred Polyoxotungstate. ChemBioChem 16:233.
    [4] Mauracher et al. (2014) Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal. Acta Cryst. D 70:2301.

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