%0 Journal Article
%A Liu, Qun
%A Kriksunov, Irina A.
%A Wang, Zhongwu
%A Graeff, Richard
%A Lee, Hon Cheung
%A Hao, Quan
%D 2008
%T Hierarchical and Helical Self-Assembly of ADP-Ribosyl Cyclase into Large-Scale Protein Microtubes
%U https://acs.figshare.com/articles/journal_contribution/Hierarchical_and_Helical_Self_Assembly_of_ADP_Ribosyl_Cyclase_into_Large_Scale_Protein_Microtubes/2897002
%R 10.1021/jp807990g.s001
%2 https://ndownloader.figshare.com/files/4595143
%K 4.5 Å resolution
%K microrods results
%K P 61 screw axis
%K protein microtube structures
%K building blocks
%K 5.6 nm
%K multifunctional nanobuilding blocks
%K scanning electron microscopy
%K 35.6 nm
%K protein nanochains
%X Proteins are macromolecules with characteristic structures and biological functions. It is extremely challenging to obtain protein microtube structures through self-assembly as proteins are very complex and flexible. Here we present a strategy showing how a specific protein, ADP-ribosyl cyclase, helically self-assembles from monomers into hexagonal nanochains and further to highly ordered crystalline microtubes. The structures of protein nanochains and consequently self-assembled superlattice were determined by X-ray crystallography at 4.5 Å resolution and imaged by scanning electron microscopy. The protein initially forms into dimers that have a fixed size of 5.6 nm, and then, helically self-assembles into 35.6 nm long hexagonal nanochains. One such nanochain consists of six dimers (12 monomers) that stack in order by a pseudo P61 screw axis. Seven nanochains produce a series of large-scale assemblies, nanorods, forming the building blocks for microrods. A proposed aging process of microrods results in the formation of hollow microstructures. Synthesis and characterization of large scale self-assembled protein microtubes may pave a new pathway, capable of not only understanding the self-assembly dynamics of biological materials, but also directing design and fabrication of multifunctional nanobuilding blocks with particular applications in biomedical engineering.
%I ACS Publications