7RX5

Cryo-EM reconstruction of Form1-N2 nanotube (Form I like)

Summary for 7RX5

• Entry DOI: 10.2210/pdb7rx5/pdb
• EMDB information: 24725
• Descriptor: F1-N2 nanotube (1 entity in total)
• Functional Keywords: helical symmetry, peptide nanotube, self-assembly, de novo protein
• Biological source: Synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 3255.66

Authors

Wang, F.,Gnewou, O.M.,Solemanifar, A.,Xu, C.,Egelman, E.H.,Conticello, V.P. (deposition date: 2021-08-21, release date: 2021-09-08, Last modification date: 2025-05-14)

Primary citation

Wang, F.,Gnewou, O.,Solemanifar, A.,Conticello, V.P.,Egelman, E.H.
Cryo-EM of Helical Polymers.
Chem.Rev., 122:14055-14065, 2022

PubMed Abstract: While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study synthetic soft matter noncovalent polymers has been much more limited. This has mainly been due to the lack of familiarity with cryo-EM in the materials science and chemistry communities, in contrast to the fact that cryo-EM was developed as a biological technique. Nevertheless, the relatively few structures of self-assembled peptide nanotubes and ribbons solved at near-atomic resolution by cryo-EM have demonstrated that cryo-EM should be the method of choice for a structural analysis of synthetic helical filaments. In addition, cryo-EM has also demonstrated that the self-assembly of soft matter polymers has enormous potential for polymorphism, something that may be obscured by techniques such as scattering and spectroscopy. These cryo-EM structures have revealed how far we currently are from being able to predict the structure of these polymers due to their chaotic self-assembly behavior.

PubMed: 35133794
DOI: 10.1021/acs.chemrev.1c00753

Experimental method

ELECTRON MICROSCOPY (3.4 Å)