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P2, the major capsid protein of bacteriophage PM2, adopts the double β-barrel fold characteristic of the PRD1-adenoviral lineage. The 2.5 Å resolution X-ray data obtained by analysis of the two major lattices of a multiple crystal of P2 were phased by molecular replacement, using as a search model structure factors to 7.6 Å resolution obtained from electron density cut from the map of the entire PM2 virion. Phase extension to 2.5 Å resolution used solely sixfold cycling averaging and solvent flattening. This represents an atypical example of an oligomeric protein for which the structure has been determined at high resolution by bootstrapping from low-resolution initial phases.

Original publication

DOI

10.1107/S0907444911002277

Type

Journal article

Journal

Acta Crystallogr D Biol Crystallogr

Publication Date

03/2011

Volume

67

Pages

228 - 232

Keywords

Bacteriophages, Capsid Proteins, Crystallography, X-Ray, Models, Molecular, Protein Structure, Quaternary, Protein Structure, Tertiary