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

0421902 - ÚOCHB 2014 RIV US eng J - Článek v odborném periodiku
Němeček, D. - Plevka, P. - Bouřa, Evžen
Using cryoEM Reconstruction and Phase Extension to Determine Crystal Structure of Bacteriophage .fi.6 Major Capsid Protein.
Protein Journal. Roč. 32, č. 8 (2013), s. 635-640. ISSN 1572-3887. E-ISSN 1573-4943
GRANT EU: European Commission(XE) 333916 - STARPI4K
Institucionální podpora: RVO:61388963
Klíčová slova: molecular replacement * cryo-electron microscopy * non-crystallographic symmetry
Kód oboru RIV: CE - Biochemie
Impakt faktor: 1.039, rok: 2013

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.
Trvalý link: http://hdl.handle.net/11104/0228154