@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}
}
