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Using cryoEM Reconstruction and Phase Extension to Determine Crystal Structure of Bacteriophage .fi.6 Major Capsid Protein

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00421902" target="_blank" >RIV/61388963:_____/13:00421902 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1007/s10930-013-9526-x" target="_blank" >http://dx.doi.org/10.1007/s10930-013-9526-x</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s10930-013-9526-x" target="_blank" >10.1007/s10930-013-9526-x</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Using cryoEM Reconstruction and Phase Extension to Determine Crystal Structure of Bacteriophage .fi.6 Major Capsid Protein

  • Original language description

    Bacteriophage I center dot 6 is a double-stranded RNA virus that has been extensively studied as a model organism. Here we describe structure determination of I center dot 6 major capsid protein P1. The protein crystallized in base centered orthorhombicspace group C222(1). Matthews's coefficient indicated that the crystals contain from four to seven P1 subunits in the crystallographic asymmetric unit. The self-rotation function had shown presence of fivefold axes of non-crystallographic symmetry in thecrystals. Thus, electron density map corresponding to a P1 pentamer was excised from a previously determined cryoEM reconstruction of the I center dot 6 procapsid at 7 resolution and used as a model for molecular replacement. The phases for reflectionsat higher than 7 resolution were obtained by phase extension employing the fivefold non-crystallographic symmetry present in the crystal. The averaged 3.6 -resolution electron density map was of sufficient quality to allow model building.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Protein Journal

  • ISSN

    1572-3887

  • e-ISSN

  • Volume of the periodical

    32

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    6

  • Pages from-to

    635-640

  • UT code for WoS article

    000328080300006

  • EID of the result in the Scopus database