@article {45965,
	title = {A conformational switch in bacteriophage p22 portal protein primes genome injection.},
	journal = {Molecular Cell},
	volume = {29},
	year = {2008},
	month = {2008 Feb 15},
	pages = {376-83},
	abstract = {<p>Double-stranded DNA (dsDNA) viruses such as herpesviruses and bacteriophages infect by delivering their genetic material into cells, a task mediated by a DNA channel called "portal protein." We have used electron cryomicroscopy to determine the structure of bacteriophage P22 portal protein in both the procapsid and mature capsid conformations. We find that, just as the viral capsid undergoes major conformational changes during virus maturation, the portal protein switches conformation from a procapsid to a mature phage state upon binding of gp4, the factor that initiates tail assembly. This dramatic conformational change traverses the entire length of the DNA channel, from the outside of the virus to the inner shell, and erects a large dome domain directly above the DNA channel that binds dsDNA inside the capsid. We hypothesize that this conformational change primes dsDNA for injection and directly couples completion of virus morphogenesis to a new cycle of infection.</p>
},
	keywords = {Bacteriophage P22, Binding Sites, Capsid Proteins, DNA, Viral, Genome, Models, Molecular, Protein Binding, Protein Conformation, Viral Tail Proteins},
	issn = {1097-2765},
	doi = {10.1016/j.molcel.2007.11.034},
	author = {Zheng, Hongjin and Olia, Adam S and Gonen, Melissa and Andrews, Simeon and Cingolani, Gino and Gonen, Tamir}
}
@article {45966,
	title = {Electron crystallography of aquaporins.},
	journal = {IUBMB Life},
	volume = {60},
	year = {2008},
	month = {2008 Jul},
	pages = {430-6},
	abstract = {<p>Aquaporins are a family of ubiquitous membrane proteins that form a pore for the permeation of water. Both electron and X-ray crystallography played major roles in determining the atomic structures of a number of aquaporins. This review focuses on electron crystallography, and its contribution to the field of aquaporin biology. We briefly discuss electron crystallography and the two-dimensional crystallization process. We describe features of aquaporins common to both electron and X-ray crystallographic structures; as well as some structural insights unique to electron crystallography, including aquaporin junction formation and lipid-protein interactions.</p>
},
	keywords = {Animals, Aquaporins, Cell Membrane, Crystallization, Crystallography, Crystallography, X-Ray, Electrons, Humans, Lipids, Models, Molecular, Protein Conformation, Protein Folding, Proteins, Water},
	issn = {1521-6551},
	doi = {10.1002/iub.53},
	author = {Andrews, Simeon and Reichow, Steve L and Gonen, Tamir}
}
