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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Protein Journal

ISSN

1572-3887

e-ISSN

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Svazek periodika

32

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

6

Strana od-do

635-640

Kód UT WoS článku

000328080300006

EID výsledku v databázi Scopus

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