@article {47711,
	title = {Accurate design of megadalton-scale two-component icosahedral protein complexes.},
	journal = {Science (New York, N.Y.)},
	volume = {353},
	year = {2016},
	month = {2016 Jul 22},
	pages = {389-94},
	abstract = {<p>Nature provides many examples of self- and co-assembling protein-based molecular machines, including icosahedral protein cages that serve as scaffolds, enzymes, and compartments for essential biochemical reactions and icosahedral virus capsids, which encapsidate and protect viral genomes and mediate entry into host cells. Inspired by these natural materials, we report the computational design and experimental characterization of co-assembling, two-component, 120-subunit icosahedral protein nanostructures with molecular weights (1.8 to 2.8 megadaltons) and dimensions (24 to 40 nanometers in diameter) comparable to those of small viral capsids. Electron microscopy, small-angle x-ray scattering, and x-ray crystallography show that 10 designs spanning three distinct icosahedral architectures form materials closely matching the design models. In vitro assembly of icosahedral complexes from independently purified components occurs rapidly, at rates comparable to those of viral capsids, and enables controlled packaging of molecular cargo through charge complementarity. The ability to design megadalton-scale materials with atomic-level accuracy and controllable assembly opens the door to a new generation of genetically programmable protein-based molecular machines.</p>
},
	issn = {1095-9203},
	doi = {10.1126/science.aaf8818},
	author = {Bale, Jacob B and Gonen, Shane and Liu, Yuxi and Sheffler, William and Ellis, Daniel and Thomas, Chantz and Cascio, Duilio and Yeates, Todd O and Gonen, Tamir and King, Neil P and Baker, David}
}
@article {46923,
	title = {Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.},
	journal = {Protein Science},
	volume = {24},
	year = {2015},
	month = {2015 Jul 15},
	pages = {1695-701},
	abstract = {<p>We recently reported the development of a computational method for the design of co-assembling, multi-component protein nanomaterials. While four such materials were validated at high-resolution by X-ray crystallography, low yield of soluble protein prevented X-ray structure determination of a fifth designed material, T33-09. Here we report the design and crystal structure of T33-31, a variant of T33-09 with improved soluble yield resulting from redesign efforts focused on mutating solvent-exposed side chains to charged amino acids. The structure is found to match the computational design model with atomic-level accuracy, providing further validation of the design approach and demonstrating a simple and potentially general means of improving the yield of designed protein nanomaterials. This article is protected by copyright. All rights reserved.</p>
},
	issn = {1469-896X},
	doi = {10.1002/pro.2748},
	author = {Bale, Jacob B and Park, Rachel U and Liu, Yuxi and Gonen, Shane and Gonen, Tamir and Cascio, Duilio and King, Neil P and Yeates, Todd O and Baker, David}
}
