Improved interface packing and design opportunities revealed by CryoEM analysis of a designed protein nanocage.

ABSTRACT: Symmetric protein assemblies play important roles in nature which makes them an attractive target for engineering. De novo symmetric protein complexes can be created through computational protein design to tailor their properties from first principles, and recently several protein nanocages have been created by bringing together protein components through hydrophobic interactions. Accurate experimental structures of newly-developed proteins are essential to validate their design, improve assembly stability, and tailor downstream applications. We describe the CryoEM structure of the nanocage I3-01, at an overall resolution of 3.5 Å. I3-01, comprising 60 aldolase subunits arranged with icosahedral symmetry, has resisted high-resolution characterization. Some key differences between th

SUBMITTER: McCarthy S 

PROVIDER: S-EPMC9801105 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature