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The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms

The use of the tellurium-centered Anderson−Evans polyoxotungstate [TeW(6)O(24)](6−) (TEW) as a crystallization additive has been described. Here, we present the use of TEW as an additive in the crystallization screening of the nucleotide binding domain (NBD) of HSP70. Crystallization screening of th...

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Autores principales: Mac Sweeney, Aengus, Chambovey, Alain, Wicki, Micha, Müller, Manon, Artico, Nadia, Lange, Roland, Bijelic, Aleksandar, Breibeck, Joscha, Rompel, Annette
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6021075/
https://www.ncbi.nlm.nih.gov/pubmed/29949628
http://dx.doi.org/10.1371/journal.pone.0199639
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author Mac Sweeney, Aengus
Chambovey, Alain
Wicki, Micha
Müller, Manon
Artico, Nadia
Lange, Roland
Bijelic, Aleksandar
Breibeck, Joscha
Rompel, Annette
author_facet Mac Sweeney, Aengus
Chambovey, Alain
Wicki, Micha
Müller, Manon
Artico, Nadia
Lange, Roland
Bijelic, Aleksandar
Breibeck, Joscha
Rompel, Annette
author_sort Mac Sweeney, Aengus
collection PubMed
description The use of the tellurium-centered Anderson−Evans polyoxotungstate [TeW(6)O(24)](6−) (TEW) as a crystallization additive has been described. Here, we present the use of TEW as an additive in the crystallization screening of the nucleotide binding domain (NBD) of HSP70. Crystallization screening of the HSP70 NBD in the absence of TEW using a standard commercial screen resulted in a single crystal form. An identical crystallization screen of the HSP70 NBD in the presence of TEW resulted in both the “TEW free” crystal form and an additional crystal form with a different crystal packing. TEW binding was observed in both crystal forms, either as a well-defined molecule or in overlapping alternate positions suggesting translational disorder. The structures were solved by both molecular replacement and single wavelength anomalous diffraction (SAD) using the anomalous signal of a single bound molecule of TEW. This study adds one more example of TEW binding to a protein and influencing its crystallization behavior.
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spelling pubmed-60210752018-07-07 The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms Mac Sweeney, Aengus Chambovey, Alain Wicki, Micha Müller, Manon Artico, Nadia Lange, Roland Bijelic, Aleksandar Breibeck, Joscha Rompel, Annette PLoS One Research Article The use of the tellurium-centered Anderson−Evans polyoxotungstate [TeW(6)O(24)](6−) (TEW) as a crystallization additive has been described. Here, we present the use of TEW as an additive in the crystallization screening of the nucleotide binding domain (NBD) of HSP70. Crystallization screening of the HSP70 NBD in the absence of TEW using a standard commercial screen resulted in a single crystal form. An identical crystallization screen of the HSP70 NBD in the presence of TEW resulted in both the “TEW free” crystal form and an additional crystal form with a different crystal packing. TEW binding was observed in both crystal forms, either as a well-defined molecule or in overlapping alternate positions suggesting translational disorder. The structures were solved by both molecular replacement and single wavelength anomalous diffraction (SAD) using the anomalous signal of a single bound molecule of TEW. This study adds one more example of TEW binding to a protein and influencing its crystallization behavior. Public Library of Science 2018-06-27 /pmc/articles/PMC6021075/ /pubmed/29949628 http://dx.doi.org/10.1371/journal.pone.0199639 Text en © 2018 Mac Sweeney et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Mac Sweeney, Aengus
Chambovey, Alain
Wicki, Micha
Müller, Manon
Artico, Nadia
Lange, Roland
Bijelic, Aleksandar
Breibeck, Joscha
Rompel, Annette
The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms
title The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms
title_full The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms
title_fullStr The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms
title_full_unstemmed The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms
title_short The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms
title_sort crystallization additive hexatungstotellurate promotes the crystallization of the hsp70 nucleotide binding domain into two different crystal forms
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6021075/
https://www.ncbi.nlm.nih.gov/pubmed/29949628
http://dx.doi.org/10.1371/journal.pone.0199639
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