NĚMEČEK, Daniel, Pavel PLEVKA and Evzen BOURA. Using cryoEM Reconstruction and Phase Extension to Determine Crystal Structure of Bacteriophage I center dot 6 Major Capsid Protein. The Protein Journal. NEW YORK: SPRINGER, 2013, vol. 32, No 8, p. 635-640. ISSN 1572-3887. Available from: https://dx.doi.org/10.1007/s10930-013-9526-x.
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Basic information
Original name Using cryoEM Reconstruction and Phase Extension to Determine Crystal Structure of Bacteriophage I center dot 6 Major Capsid Protein
Authors NĚMEČEK, Daniel (203 Czech Republic, guarantor, belonging to the institution), Pavel PLEVKA (203 Czech Republic, belonging to the institution) and Evzen BOURA (203 Czech Republic).
Edition The Protein Journal, NEW YORK, SPRINGER, 2013, 1572-3887.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 1.039
RIV identification code RIV/00216224:14740/13:00072307
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1007/s10930-013-9526-x
UT WoS 000328080300006
Keywords in English Molecular replacement; Cryo-electron microscopy; Non-crystallographic symmetry; Virus capsid protein; Phase extension
Tags ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 8/4/2014 01:46.
Abstract
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 orthorhombic space 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 the crystals. 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 reflections at 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.
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