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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

DOI: 10.1107/S0907444911002277 DOI Help
PMID: 21358054 PMID Help

Authors: Nicola Abrescia (CIC bioGUNE; University of Oxford; IKERBASQUE, Basque Foundation for Science) , Jonathan Grimes (University of Oxford; Diamond Light Source) , Hanna M. Oksanen (University of Helsinki) , Jaana K. H. Bamford (University of Jyväskylä) , Dennis H. Bamford (University of Helsinki) , David I. Stuart (Diamond Light Source; University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Biological Crystallography , VOL 67 (3) , PAGES 228-232

State: Published (Approved)
Published: January 2011

Abstract: P2, the major capsid protein of bacteriophage PM2, adopts the double beta-barrel fold characteristic of the PRD1-adenoviral lineage. The 2.5 A 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 A resolution obtained from electron density cut from the map of the entire PM2 virion. Phase extension to 2.5 A 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.

Journal Keywords: Virus Structure; Phasing Methods; Data Collection; Noncrystallographic Symmetry

Diamond Keywords: Bacteriophages; Viruses

Subject Areas: Biology and Bio-materials

Facility: BM14 at ESRF

Added On: 28/03/2011 14:54

Discipline Tags:

Structural biology Life Sciences & Biotech

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