» Sign in / Register

XP Screen: The Protein Crystal Glue

visit product page

Discover our XP Screen with TEW – the protein crystal glue – and benefit from improved crystal quality and resolution!

XP Screen with TEW

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. It exhibits a planar structure with six tungsten atoms, being able to improve crystal quality and resolution while providing a valuable 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]

The XP Screen consists of the 96 most prominent crystallization conditions plus TEW to provide an environment to increase the chances of crystallization and improve crystal diffraction quality.

Christin Reuter

E-Mail Christin for technical inquiries or further information: xtals@jenabioscience.com

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.