From high-resolution AFM topographs to atomic models of supramolecular assemblies. Academic Article uri icon

Overview

abstract

  • Atomic force microscopy (AFM) has developed into a powerful tool in membrane biology. AFM features an outstanding signal-to-noise ratio that allows substructures on individual macromolecules to be visualized. Most recently, AFM topographs have shown the supramolecular assembly of the bacterial photosynthetic complexes in native membranes. Here, we have determined the translational and rotational degrees of freedom of the complexes in AFM images of multi-protein assemblies, in order to build realistic atomic models of supramolecular assemblies by docking high-resolution structures into the topographs. Membrane protein assemblies of megadalton size comprising several hundreds of polypeptide chains and pigments were built with Angstrom precision.

publication date

  • February 17, 2007

Research

keywords

  • Microscopy, Atomic Force
  • Multiprotein Complexes

Identity

Scopus Document Identifier

  • 34447638509

Digital Object Identifier (DOI)

  • 10.1016/j.jsb.2007.01.021

PubMed ID

  • 17399998

Additional Document Info

volume

  • 159

issue

  • 2