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XP Screen

Crystallization Screen for high TEW concentrations

Cat. No. Amount Price (EUR) Buy / Note
CS-350 96 solutions (1,7 ml each) 457,60 Add to Basket/Quote Add to Notepad

 

For general laboratory use.

Shipping: shipped at ambient temperature

Storage Conditions: store at 8-10 °C

Shelf Life: 12 months

Description:
The additive Anderson-Evans polyoxotungstate (TEW) [TeW6O24]6− has been shown to promote crystal contacts, improve crystal quality, and provide a valuable anomalous signal for phase determination due to its 6 tungsten atoms. It has successfully induced protein crystallization even at low concentrations of 1 mM. However, our own experiments have shown that a higher concentration of 5 or 10 mM TEW can significantly increase crystallizability even further.
The XP Up Screen offers 96 of the most common crystallization conditions that have been proven to be successfully improved with up to 10 mM TEW. The solutions are stable in the long term in the presence of up to 10 mM TEW, thus enabling maximum flexibility without compromise.

The Anderson-Evans polyoxotungstate (TEW), 20 mg, Cat.-No. X-TEW-20 is available separately.

Content:
96 screening solutions x 1.7 ml each, optimized for high TEW concentrations

The exact composition of each buffer is listed under the links “Screen Formulation”.
All solutions are sterile filtered (0.2 μm), filled under sterile conditions and contain 0.1% ProClinTM 950 as preservative to prevent the growth of microbes. (ProClin is a trademark of LANXESS Corp.)

Selected Literature Citations of XP Screen

  • 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.

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BIOZ Product Citations:

Selected 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) Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases. Proc. Natl. Acad. Sci. 113:E1806.
[3] 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.
[4] Molitor et al. (2015) Crystallization and preliminary crystallographic analysis of latent, active and recombinantly expressed aurone synthase, a polyphenol oxidase, from Coreopsis grandiflora. Acta Cryst. F 71:746.
[5] Bijelic et al. (2015) Hen Egg-White Lysozyme Crystallisation: Protein Stacking and Structure Stability Enhanced by a Tellurium(VI)-Centred Polyoxotungstate. ChemBioChem 16:233.
[6] Mauracher et al. (2014) Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal. Acta Cryst. D 70:2301.
[7] Mauracher et al. (2014) Crystallization and preliminary X-ray crystallographic analysis of latent isoform PPO4 mushroom (Agaricus bisporus) tyrosinase. Acta Cryst. F 70:263.