Diffraction quality crystals of PRD1, a 66-MDa dsDNA virus with an internal membrane.
It has proved difficult to obtain well diffracting single crystals of macromolecular complexes rich in lipid. We report here the path that has led to crystals of the bacteriophage PRD1, a particle containing approximately 2,000 protein subunits from 18 different protein species, around 10 of which are integral membrane proteins associated with a host-derived lipid bilayer of some 12,500 lipid molecules. These crystals are capable of diffracting X-rays to Bragg spacings below 4A. It is hoped that some lessons learned from PRD1 will be applicable to other lipidic systems and that these crystals will allow, as a proof of principle, the determination of the structure of the virus in terms of a detailed atomic model.
Bamford
Jaana K H
JK
Institute of Biotechnology and Department of Biosciences, Biocenter 2, University of Helsinki, P.O. Box 56, Viikinkaari 5, 00014 University of Helsinki, Finland. jaana.bamford@helsinki.fi
Cockburn
Joseph J B
JJ
Diprose
Jonathan
J
Grimes
Jonathan M
JM
Sutton
Geoff
G
Stuart
David I
DI
Bamford
Dennis H
DH
D025622:Bacteriophage PRD1 / Q000737:chemistry*; D001435:Bacteriophages / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D018360:Crystallography, X-Ray; D004279:DNA, Viral / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D008051:Lipid Bilayers / Q000737:chemistry; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry; D016366:Open Reading Frames; D019779:Salmonella enterica / Q000378:metabolism; D012542:Scattering, Radiation
D004279:DNA, Viral; D008051:Lipid Bilayers; D008055:Lipids