Three-dimensional reconstruction of individual helical nano-filament structures from atomic force microscopy topographs

Autor: Liisa Lutter, Louise C. Serpell, Mick F. Tuite, Christopher J. Serpell, Wei-Feng Xue
Rok vydání: 2020
Předmět:
0301 basic medicine
Amyloid
Materials science
Cantilever
QH301-705.5
Ensemble averaging
Nanofibers
macromolecular substances
02 engineering and technology
Microscopy
Atomic Force
010402 general chemistry
01 natural sciences
General Biochemistry
Genetics and Molecular Biology
Protein filament
03 medical and health sciences
Cellular and Molecular Neuroscience
Imaging
Three-Dimensional
Optics
image analysis
Nano
Humans
Nanotechnology
amyloid fibril structure
Biology (General)
Image resolution
QC
030304 developmental biology
0303 health sciences
atomic force microscopy
business.industry
3D reconstruction
technology
industry
and agriculture
General Medicine
021001 nanoscience & nanotechnology
Nanostructures
0104 chemical sciences
030104 developmental biology
Structural biology
tip-sample convolution
Deconvolution
QP517
Peptides
0210 nano-technology
business
Zdroj: Biomolecular Concepts, Vol 11, Iss 1, Pp 102-115 (2020)
ISSN: 1868-503X
1868-5021
DOI: 10.1515/bmc-2020-0009
Popis: Atomic force microscopy, AFM, is a powerful tool that can produce detailed topographical images of individual nano-structures with a high signal-to-noise ratio without the need for ensemble averaging. However, the application of AFM in structural biology has been hampered by the tip-sample convolution effect, which distorts images of nano-structures, particularly those that are of similar dimensions to the cantilever probe tips used in AFM. Here we show that the tip-sample convolution results in a feature-dependent and non-uniform distribution of image resolution on AFM topographs. We show how this effect can be utilised in structural studies of nano-sized upward convex objects such as spherical or filamentous molecular assemblies deposited on a flat surface, because it causes ‘magnification’ of such objects in AFM topographs. Subsequently, this enhancement effect is harnessed through contact-point based deconvolution of AFM topographs. Here, the application of this approach is demonstrated through the 3D reconstruction of the surface envelope of individual helical amyloid filaments without the need of cross-particle averaging using the contact-deconvoluted AFM topographs. Resolving the structural variations of individual macromolecular assemblies within inherently heterogeneous populations is paramount for mechanistic understanding of many biological phenomena such as amyloid toxicity and prion strains. The approach presented here will also facilitate the use of AFM for high-resolution structural studies and integrative structural biology analysis of single molecular assemblies.
Databáze: OpenAIRE
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