title: Using cryoEM reconstruction and phase extension to determine crystal structure of bacteriophage ϕ6 major capsid protein.
abstract: Bacteriophage ϕ6 is a double-stranded RNA virus that has been extensively studied as a model organism. Here we describe structure determination of ϕ6 major capsid protein P1. The protein crystallized in base centered orthorhombic space group C2221. 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 ϕ6 procapsid at 7 Å resolution and used as a model for molecular replacement. The phases for reflections at higher than 7 Å resolution were obtained by phase extension employing the fivefold non-crystallographic symmetry present in the crystal. The averaged 3.6 Å-resolution electron density map was of sufficient quality to allow model building.
authors.affiliation: Central European Institute of Technology, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
authors.forename: Daniel
authors.initials: D
authors.lastname: Nemecek
authors.forename: Pavel
authors.initials: P
authors.lastname: Plevka
authors.forename: Evzen
authors.initials: E
authors.lastname: Boura
mesh_terms: D017126:Bacteriophage phi 6 / Q000737:chemistry*; D036022:Capsid Proteins / Q000737:chemistry*; D020285:Cryoelectron Microscopy; D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D036022:Capsid Proteins