Format

Send to

Choose Destination
See comment in PubMed Commons below
ACS Nano. 2013 Jun 25;7(6):4946-53. doi: 10.1021/nn400263j. Epub 2013 Jun 3.

Self-assembly of "S-bilayers", a step toward expanding the dimensionality of S-layer assemblies.

Author information

1
Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.

Abstract

Protein-based assemblies with ordered nanometer-scale features in three dimensions are of interest as functional nanomaterials but are difficult to generate. Here we report that a truncated S-layer protein assembles into stable bilayers, which we characterized using cryogenic-electron microscopy, tomography, and X-ray spectroscopy. We find that emergence of this supermolecular architecture is the outcome of hierarchical processes; the proteins condense in solution to form 2-D crystals, which then stack parallel to one another to create isotropic bilayered assemblies. Within this bilayered structure, registry between lattices in two layers was disclosed, whereas the intrinsic symmetry in each layer was altered. Comparison of these data to images of wild-type SbpA layers on intact cells gave insight into the interactions responsible for bilayer formation. These results establish a platform for engineering S-layer assemblies with 3-D architecture.

PMID:
23705800
DOI:
10.1021/nn400263j
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society
    Loading ...
    Support Center