Crystallization and preliminary crystallographic analysis of the major capsid proteins VP16 and VP17 of bacteriophage P23-77
Rissanen, 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. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(5), 580-583. https://doi.org/10.1107/S1744309112010330
Julkaistu sarjassa
Acta Crystallographica Section F: Structural Biology and Crystallization CommunicationsTekijät
Päivämäärä
2012Oppiaine
Solu- ja molekyylibiologiaBiologisten vuorovaikutusten huippututkimusyksikköVirologian huippuyksikköCell and Molecular BiologyCentre of Excellence in Biological Interactions ResearchCentre of Excellence in Virus ResearchTekijänoikeudet
© 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.
Members 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
...
Julkaisija
International Union of Crystallography (IUCr)ISSN Hae Julkaisufoorumista
1744-3091Asiasanat
Alkuperäislähde
http://journals.iucr.org/f/issues/2012/05/00/nj5117/index.htmlJulkaisu tutkimustietojärjestelmässä
https://converis.jyu.fi/converis/portal/detail/Publication/21663366
Metadata
Näytä kaikki kuvailutiedotKokoelmat
Lisenssi
Ellei muuten mainita, aineiston lisenssi on © 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.
Samankaltainen aineisto
Näytetään aineistoja, joilla on samankaltainen nimeke tai asiasanat.
-
Interactions between Rainbow Trout Eyed Eggs and Flavobacterium spp. Using a Bath Challenge Model : Preliminary Evaluation of Bacteriophages as Pathogen Control Agents
Donati, Valentina L.; Dalsgaard, Inger; Runtuvuori-Salmela, Anniina; Kunttu, Heidi; Jørgensen, Johanna; Castillo, Daniel; Sundberg, Lotta-Riina; Middelboe, Mathias; Madsen, Lone (MDPI AG, 2021)The microbial community surrounding fish eyed eggs can harbor pathogenic bacteria. In this study we focused on rainbow trout (Oncorhynchus mykiss) eyed eggs and the potential of bacteriophages against the pathogenic bacteria ... -
Immunodetection of VP11, the minor capsid protein of thermophilic bacteriophage P23-77
Moilanen, Anni (2015)VP11 on termofiilisen bakteriofagin P23-77 kapsidiproteiini ja se muodostaa ikosahedraalisen kapsidirakenteen yhdessä pääkapsidiproteiinien, virusproteiini (VP)16 ja VP17, kanssa. VP11 tarkkaa paikkaa ja toimintaa kapsidissa ... -
Viruses are ancient parasites that have influenced the evolution of contemporary and archaic forms of life
Jalasvuori, Matti (University of Jyväskylä, 2010) -
An ancient virus type from extreme environments
Rissanen, Ilona (University of Jyväskylä, 2014) -
Thermus bacteriophage P23-77 : key member of a novel, but ancient family of viruses from extreme environments
Pawlowski, Alice (University of Jyväskylä, 2015)
Ellei toisin mainittu, julkisesti saatavilla olevia JYX-metatietoja (poislukien tiivistelmät) saa vapaasti uudelleenkäyttää CC0-lisenssillä.