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Title: Preliminary crystallographic analysis of the major capsid protein P2 of the lipid-containing bacteriophage PM2

Abstract

The viral capsid protein P2 of bacteriophage PM2 has been crystallized. Preliminary X-ray analysis demonstrates the position and orientation of the two trimers in the asymmetric unit. PM2 (Corticoviridae) is a dsDNA bacteriophage which contains a lipid membrane beneath its icosahedral capsid. In this respect it resembles bacteriophage PRD1 (Tectiviridae), although it is not known whether the similarity extends to the detailed molecular architecture of the virus, for instance the fold of the major coat protein P2. Structural analysis of PM2 has been initiated and virus-derived P2 has been crystallized by sitting-nanodrop vapour diffusion. Crystals of P2 have been obtained in space group P2{sub 1}2{sub 1}2, with two trimers in the asymmetric unit and unit-cell parameters a = 171.1, b = 78.7, c = 130.1 Å. The crystals diffract to 4 Å resolution at the ESRF BM14 beamline (Grenoble, France) and the orientation of the non-crystallographic threefold axes, the spatial relationship between the two trimers and the packing of the trimers within the unit cell have been determined. The trimers form tightly packed layers consistent with the crystal morphology, possibly recapitulating aspects of the arrangement of subunits in the virus.

Authors:
 [1];  [2];  [1]; ;  [2];  [1]
  1. Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN (United Kingdom)
  2. Institute of Biotechnology and Department of Biological and Environmental Sciences, University of Helsinki, PO Box 56, Viikinkaari 5, 00014 University of Helsinki (Finland)
Publication Date:
OSTI Identifier:
22356049
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 61; Journal Issue: Pt 8; Other Information: PMCID: PMC1952355; PMID: 16511151; PUBLISHER-ID: en5116; OAI: oai:pubmedcentral.nih.gov:1952355; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALS; DIFFUSION; EUROPEAN SYNCHROTRON RADIATION FACILITY; LAYERS; MEMBRANES; MORPHOLOGY; ORIENTATION; PROTEINS; RESOLUTION; SPACE GROUPS; STOWING

Citation Formats

Abrescia, Nicola G. A., Kivelä, Hanna M., Grimes, Jonathan M., Bamford, Jaana K. H., Bamford, Dennis H., and Stuart, David I., E-mail: dave@strubi.ox.ac.uk. Preliminary crystallographic analysis of the major capsid protein P2 of the lipid-containing bacteriophage PM2. United Kingdom: N. p., 2005. Web. doi:10.1107/S174430910502141X.
Abrescia, Nicola G. A., Kivelä, Hanna M., Grimes, Jonathan M., Bamford, Jaana K. H., Bamford, Dennis H., & Stuart, David I., E-mail: dave@strubi.ox.ac.uk. Preliminary crystallographic analysis of the major capsid protein P2 of the lipid-containing bacteriophage PM2. United Kingdom. doi:10.1107/S174430910502141X.
Abrescia, Nicola G. A., Kivelä, Hanna M., Grimes, Jonathan M., Bamford, Jaana K. H., Bamford, Dennis H., and Stuart, David I., E-mail: dave@strubi.ox.ac.uk. Mon . "Preliminary crystallographic analysis of the major capsid protein P2 of the lipid-containing bacteriophage PM2". United Kingdom. doi:10.1107/S174430910502141X.
@article{osti_22356049,
title = {Preliminary crystallographic analysis of the major capsid protein P2 of the lipid-containing bacteriophage PM2},
author = {Abrescia, Nicola G. A. and Kivelä, Hanna M. and Grimes, Jonathan M. and Bamford, Jaana K. H. and Bamford, Dennis H. and Stuart, David I., E-mail: dave@strubi.ox.ac.uk},
abstractNote = {The viral capsid protein P2 of bacteriophage PM2 has been crystallized. Preliminary X-ray analysis demonstrates the position and orientation of the two trimers in the asymmetric unit. PM2 (Corticoviridae) is a dsDNA bacteriophage which contains a lipid membrane beneath its icosahedral capsid. In this respect it resembles bacteriophage PRD1 (Tectiviridae), although it is not known whether the similarity extends to the detailed molecular architecture of the virus, for instance the fold of the major coat protein P2. Structural analysis of PM2 has been initiated and virus-derived P2 has been crystallized by sitting-nanodrop vapour diffusion. Crystals of P2 have been obtained in space group P2{sub 1}2{sub 1}2, with two trimers in the asymmetric unit and unit-cell parameters a = 171.1, b = 78.7, c = 130.1 Å. The crystals diffract to 4 Å resolution at the ESRF BM14 beamline (Grenoble, France) and the orientation of the non-crystallographic threefold axes, the spatial relationship between the two trimers and the packing of the trimers within the unit cell have been determined. The trimers form tightly packed layers consistent with the crystal morphology, possibly recapitulating aspects of the arrangement of subunits in the virus.},
doi = {10.1107/S174430910502141X},
journal = {Acta Crystallographica. Section F},
number = Pt 8,
volume = 61,
place = {United Kingdom},
year = {Mon Aug 01 00:00:00 EDT 2005},
month = {Mon Aug 01 00:00:00 EDT 2005}
}