The use of low-resolution phasing followed by phase extension from 7.6 to 2.5 A resolution with noncrystallographic symmetry to solve the structure of a bacteriophage capsid protein.

Journal article

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 ...

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Authors: Abrescia, N; Grimes, J; Oksanen, H; Bamford, J; Bamford, D

• Publication status: Published
• Journal: Acta crystallographica. Section D, Biological crystallography
• Volume: 67
• Issue: Pt 3
• Pages: 228-232
• Publication date: 2011-03-01
• DOI: 10.1107/s0907444911002277
• EISSN: 1399-0047
• ISSN: 0907-4449
• Language: English
• Keywords: Capsid Proteins; Protein Structure, Quaternary; Crystallography, X-Ray; Protein Structure, Tertiary; Bacteriophages; Models, Molecular