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.

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.

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 s...

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Bibliographic Details
Main Authors: Abrescia, N, Grimes, J, Oksanen, H, Bamford, J, Bamford, D, Stuart, D
Format: Journal article
Language:English
Published: 2011
Description
Summary: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.

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