Evidence map›Paper›PMID 25521080›Full record

ArticleChembiochem : a European journal of chemical biology2015

Hen egg-white lysozyme crystallisation: protein stacking and structure stability enhanced by a Tellurium(VI)-centred polyoxotungstate.

Aleksandar Bijelic, Christian Molitor, Stephan G Mauracher, Rami Al-Oweini, Ulrich Kortz, Annette Rompel

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

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0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Synthesis and characterization of the `Japanese rice-ball'-shaped Molybdenum Blue NaActa crystallographica. Section C, Structural chemistry · 2022
    Article
  4. Conformational flexibility in the zinc solute-binding protein ZnuA.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  5. Article
  6. Lysozyme Improves the Inhibitory Effects ofFrontiers in nutrition · 2021
    Article
  7. Multivalent ions and biomolecules: Attempting a comprehensive perspective.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020
    Review
  8. Article
  9. The Chaotropic Effect as an Assembly Motif in Chemistry.Angewandte Chemie (International ed. in English) · 2018
    Review
  10. The P-type ATPase inhibiting potential of polyoxotungstates.Metallomics : integrated biometal science · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. In situ formation of the first proteinogenically functionalized [TeWChemical communications (Cambridge, England) · 2016
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Aleksandar BijelicInstitut für Biophysikalische Chemie, Fakultät für Chemie, Universität Wien, Althanstrasse 14, 1090 Wien (Austria).
Christian Molitor
Stephan G Mauracher
Rami Al-Oweini
Ulrich Kortz
Annette Rompel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As synchrotron radiation becomes more intense, detectors become faster and structure-solving software becomes more elaborate, obtaining single crystals suitable for data collection is now the bottleneck in macromolecular crystallography. Hence, there is a need for novel and advanced crystallisation agents with the ability to crystallise proteins that are otherwise challenging. Here, an Anderson-Evans-type polyoxometalate (POM), specifically Na6 [TeW6 O24 ]⋅22 H2 O (TEW), is employed as a crystallisation additive. Its effects on protein crystallisation are demonstrated with hen egg-white lysozyme (HEWL), which co-crystallises with TEW in the vicinity (or within) the liquid-liquid phase separation (LLPS) region. The X-ray structure (PDB ID: 4PHI) determination revealed that TEW molecules are part of the crystal lattice, thus demonstrating specific binding to HEWL with electrostatic interactions and hydrogen bonds. The negatively charged TEW polyoxotungstate binds to sites with a positive electrostatic potential located between two (or more) symmetry-related protein chains. Thus, TEW facilitates the formation of protein-protein interfaces of otherwise repulsive surfaces, and thereby the realisation of a stable crystal lattice. In addition to retaining the isomorphicity of the protein structure, the anomalous scattering of the POMs was used for macromolecular phasing. The results suggest that hexatungstotellurate(VI) has great potential as a crystallisation additive to promote both protein crystallisation and structure elucidation.

Indexed as

CrystallizationCrystallography, X-RayMuramidaseOxidesProtein ConformationProtein StabilityStatic ElectricityTelluriumTungstenTungsten Compoundshen egg lysozymeMuramidaseOxidesTelluriumTungstenTungsten CompoundsAnderson-Evanselectrostatic interactionshen egg-white lysozymepolyoxometalatesprotein structures

Identifiers

PMID25521080
PMCPMC4498469

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.