MersV1, Pmc, Corpus, bibRecord, 000985

Crystallographic analysis of the N‐terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein

Identifieur interne : 000985 ( Pmc/Corpus ); précédent : 000984; suivant : 000986

Crystallographic analysis of the N‐terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein

Auteurs : Yong-Sheng Wang ; Chung-Ke Chang ; Ming-Hon Hou

Source :

Acta Crystallographica. Section F, Structural Biology Communications [ 2053-230X ] ; 2015.

RBID : PMC:4528927

Abstract

The N‐terminal domain of the nucleocapsid protein from Middle East respiratory syndrome coronavirus (MERS‐CoV NP‐NTD) contains many positively charged residues and has been identified to be responsible for RNA binding during ribonucleocapsid formation by the virus. In this study, the crystallization and crystallographic analysis of MERS‐CoV NP‐NTD (amino acids 39–165), with a molecular weight of 14.7 kDa, are reported. MERS‐CoV NP‐NTD was crystallized at 293 K using PEG 3350 as a precipitant and a 94.5% complete native data set was collected from a cooled crystal at 77 K to 2.63 Å resolution with an overall R_merge of 9.6%. The crystals were monoclinic and belonged to space group P2₁, with unit‐cell parameters a = 35.60, b = 109.64, c = 91.99 Å, β = 101.22°. The asymmetric unit contained four MERS‐CoV NP‐NTD molecules.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4528927

DOI: 10.1107/S2053230X15010146
PubMed: 26249685
PubMed Central: 4528927

Links to Exploration step

PMC:4528927

Le document en format XML

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 nucleocapsid protein</title>
<author><name sortKey="Wang, Yong Heng" sort="Wang, Yong Heng" uniqKey="Wang Y" first="Yong-Sheng" last="Wang">Yong-Sheng Wang</name>
</author>
<author><name sortKey="Chang, Chung E" sort="Chang, Chung E" uniqKey="Chang C" first="Chung-Ke" last="Chang">Chung-Ke Chang</name>
</author>
<author><name sortKey="Hou, Ming On" sort="Hou, Ming On" uniqKey="Hou M" first="Ming-Hon" last="Hou">Ming-Hon Hou</name>
</author>
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 nucleocapsid protein</title>
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<front><div type="abstract" xml:lang="en"><p>The N‐terminal domain of the nucleocapsid protein from <italic>Middle East respiratory syndrome coronavirus</italic>
 (MERS‐CoV NP‐NTD) contains many positively charged residues and has been identified to be responsible for RNA binding during ribonucleocapsid formation by the virus. In this study, the crystallization and crystallographic analysis of MERS‐CoV NP‐NTD (amino acids 39–165), with a molecular weight of 14.7 kDa, are reported. MERS‐CoV NP‐NTD was crystallized at 293 K using PEG 3350 as a precipitant and a 94.5% complete native data set was collected from a cooled crystal at 77 K to 2.63 Å resolution with an overall <italic>R</italic>
<sub>merge</sub>
 of 9.6%. The crystals were monoclinic and belonged to space group <italic>P</italic>
2<sub>1</sub>
, with unit‐cell parameters <italic>a</italic>
 = 35.60, <italic>b</italic>
 = 109.64, <italic>c</italic>
 = 91.99 Å, β = 101.22°. The asymmetric unit contained four MERS‐CoV NP‐NTD molecules.</p>
</div>
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  <front><journal-meta><journal-id journal-id-type="nlm-ta">Acta Crystallogr F Struct Biol Commun</journal-id>
<journal-id journal-id-type="iso-abbrev">Acta Crystallogr F Struct Biol Commun</journal-id>
<journal-id journal-id-type="doi">10.1107/S2053230X</journal-id>
<journal-id journal-id-type="publisher-id">AYF2</journal-id>
<journal-title-group><journal-title>Acta Crystallographica. Section F, Structural Biology Communications</journal-title>
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<issn pub-type="epub">2053-230X</issn>
<publisher><publisher-name>International Union of Crystallography</publisher-name>
<publisher-loc>5 Abbey Square, Chester, Cheshire CH1 2HU, England</publisher-loc>
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<article-categories><subj-group subj-group-type="heading"><subject>Research Communications</subject>
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<title-group><article-title>Crystallographic analysis of the N‐terminal domain of <italic>Middle East respiratory syndrome coronavirus</italic>
 nucleocapsid protein</article-title>
<alt-title alt-title-type="right-running-head">N‐terminal domain of MERS‐CoV nucleocapsid protein</alt-title>
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<contrib-group><contrib id="cr1" contrib-type="author"><name><surname>Wang</surname>
<given-names>Yong‐Sheng</given-names>
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<contrib id="cr2" contrib-type="author"><name><surname>Chang</surname>
<given-names>Chung‐ke</given-names>
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<contrib id="cr3" contrib-type="author"><name><surname>Hou</surname>
<given-names>Ming‐Hon</given-names>
</name>
</contrib>
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<aff id="a1"><label><sup>1</sup>
</label>
Department of Life Sciences, National Chung Hsing University, Taichung 402, Taiwan</aff>
<aff id="a2"><label><sup>2</sup>
</label>
Institute of Genomics and Bioinformatics, National Chung Hsing University, Taichung 402, Taiwan</aff>
<aff id="a3"><label><sup>3</sup>
</label>
Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan</aff>
<author-notes><corresp id="correspondenceTo">Ming‐Hon Hou, e‐mail: <email>mhho@nchu.edu.tw</email>
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<year>2015</year>
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<volume>71</volume>
<issue>8</issue>
<issue-id pub-id-type="doi">10.1111/ayf2.2015.71.issue-8</issue-id>
<fpage>977</fpage>
<lpage>980</lpage>
<history><pmc-comment>supplied string: Received 18 March 2015, accepted 26 May 2015</pmc-comment>
        <date date-type="received"><day>18</day>
<month>3</month>
<year>2015</year>
</date>
<date date-type="accepted"><day>26</day>
<month>5</month>
<year>2015</year>
</date>
</history>
<permissions><copyright-statement content-type="article-copyright">International Union of Crystallography, 2015</copyright-statement>
<license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p>
</license>
</permissions>
<self-uri content-type="pdf" xlink:href="file:AYF2-71-977.pdf"></self-uri>
<abstract><p>The N‐terminal domain of the nucleocapsid protein from <italic>Middle East respiratory syndrome coronavirus</italic>
 (MERS‐CoV NP‐NTD) contains many positively charged residues and has been identified to be responsible for RNA binding during ribonucleocapsid formation by the virus. In this study, the crystallization and crystallographic analysis of MERS‐CoV NP‐NTD (amino acids 39–165), with a molecular weight of 14.7 kDa, are reported. MERS‐CoV NP‐NTD was crystallized at 293 K using PEG 3350 as a precipitant and a 94.5% complete native data set was collected from a cooled crystal at 77 K to 2.63 Å resolution with an overall <italic>R</italic>
<sub>merge</sub>
 of 9.6%. The crystals were monoclinic and belonged to space group <italic>P</italic>
2<sub>1</sub>
, with unit‐cell parameters <italic>a</italic>
 = 35.60, <italic>b</italic>
 = 109.64, <italic>c</italic>
 = 91.99 Å, β = 101.22°. The asymmetric unit contained four MERS‐CoV NP‐NTD molecules.</p>
</abstract>
<kwd-group><kwd id="k1"><italic>Middle East respiratory syndrome coronavirus</italic>
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<kwd id="k2">nucleocapsid protein</kwd>
<kwd id="k3">N‐terminal domain</kwd>
<kwd id="k4">RNA binding</kwd>
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<meta-value>2.0</meta-value>
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<body><p>The full text for this article, hosted at <ext-link ext-link-type="uri" xlink:href="http://journals.iucr.org">http://journals.iucr.org</ext-link>
, is unavailable due to technical difficulties.</p>
<sec sec-type="supplementary-material"><title>Supporting information</title>
<supplementary-material content-type="local-data"><p>Multiple sequence alignment. DOI: <ext-link ext-link-type="uri" xlink:href="http://dx.doi.org/10.1107/S2053230X15010146/wd5248sup1.pdf">http://dx.doi.org/10.1107/S2053230X15010146/wd5248sup1.pdf</ext-link>
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Crystallographic analysis of the N‐terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein

Crystallographic analysis of the N‐terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein

Source :

Abstract

Links to Exploration step

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