Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.
نویسندگان
چکیده
We recently reported the development of a computational method for the design of coassembling multicomponent 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.
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We recently reported the development of a computational method for the design of coassembling multicomponent protein nanomaterials. While four such materials were validated at highresolution 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 T3331, a variant of T3...
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ورودعنوان ژورنال:
- Protein science : a publication of the Protein Society
دوره 24 10 شماره
صفحات -
تاریخ انتشار 2015