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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
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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. |
format | Online Article Text |
id | pubmed-6021075 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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