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dc.contributor.authorRissanen, Ilona
dc.contributor.authorPawlowski, Alice
dc.contributor.authorHarlos, Karl
dc.contributor.authorGrimes, Jonathan
dc.contributor.authorStuart, David
dc.contributor.authorBamford, Jaana
dc.date.accessioned2015-11-03T07:49:25Z
dc.date.available2015-11-03T07:49:25Z
dc.date.issued2012
dc.identifier.citationRissanen, I., Pawlowski, A., Harlos, K., Grimes, J., Stuart, D., & Bamford, J. (2012). Crystallization and preliminary crystallographic analysis of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. <i>Acta Crystallographica Section F: Structural Biology and Crystallization Communications</i>, <i>68</i>(5), 580-583. <a href="https://doi.org/10.1107/S1744309112010330" target="_blank">https://doi.org/10.1107/S1744309112010330</a>
dc.identifier.otherCONVID_21663366
dc.identifier.otherTUTKAID_52410
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/47548
dc.description.abstractMembers of the diverse double--barrel lineage of viruses are identified by the conserved structure of their major coat protein. New members of this lineage have been discovered based on structural analysis and we are interested in identifying relatives that utilize unusual versions of the double--barrel fold. One candidate for such studies is P23-77, an icosahedral dsDNA bacteriophage that infects the extremophile Thermus thermophilus. P23-77 has two major coat proteins, namely VP16 and VP17, of a size consistent with a single--barrel core fold. These previously unstudied proteins have now been successfully expressed as recombinant proteins, purified and crystallized using hanging-drop and sitting-drop vapour-diffusion methods. Crystals of coat proteins VP16 and VP17 have been obtained as well as of a putative complex. In addition, virus-derived material has been crystallized. Diffraction data have been collected to beyond 3 A˚ resolution for five crystal types and structure determinations are in progress. 1
dc.language.isoeng
dc.publisherInternational Union of Crystallography (IUCr)
dc.relation.ispartofseriesActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.relation.urihttp://journals.iucr.org/f/issues/2012/05/00/nj5117/index.html
dc.subject.otherbakteriofaagit
dc.subject.otherkapsidiproteiinit
dc.subject.otherBacteriophage P23-77
dc.subject.othermajor coat proteins
dc.subject.othercrystallization
dc.subject.otherThermus thermophilus
dc.subject.otherdouble beta-barrel viral lineage
dc.subject.othercapsid proteins
dc.titleCrystallization and preliminary crystallographic analysis of the major capsid proteins VP16 and VP17 of bacteriophage P23-77
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201511023567
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineBiologisten vuorovaikutusten huippututkimusyksikköfi
dc.contributor.oppiaineVirologian huippuyksikköfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineCentre of Excellence in Biological Interactions Researchen
dc.contributor.oppiaineCentre of Excellence in Virus Researchen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2015-11-02T10:15:15Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange580-583
dc.relation.issn1744-3091
dc.relation.numberinseries5
dc.relation.volume68
dc.type.versionpublishedVersion
dc.rights.copyright© 2012 the Authors. Published by International Union of Crystallography. This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence.
dc.rights.accesslevelopenAccessfi
dc.subject.ysobakteriofagit
jyx.subject.urihttp://www.yso.fi/onto/yso/p25303
dc.rights.urlhttp://creativecommons.org/licenses/by/2.0/uk/legalcode
dc.relation.doi10.1107/S1744309112010330
dc.type.okmA1


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© 2012 the Authors. Published by International Union of Crystallography. This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence.
Except where otherwise noted, this item's license is described as © 2012 the Authors. Published by International Union of Crystallography. This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence.