Structural analysis and classification of human metaphase chromosomes by atomic force microscopy

1999 ◽  
Author(s):  
Naoaki Okamoto ◽  
Takao Okada
Keyword(s):  
Atomic Force Microscopy ◽  
Structural Analysis ◽  
Metaphase Chromosomes ◽  
Force Microscopy ◽  
Atomic Force

Chemical and Structural Analysis of Nitridated Sapphire

1997 ◽  
Vol 482 ◽  
Author(s):  
Y. Cho ◽  
S. Rouvimov ◽  
Y. Kim ◽  
Z. Liliental-Weber ◽  
E. R. Weber
Keyword(s):  
Electron Microscopy ◽  
Atomic Force Microscopy ◽  
Structural Analysis ◽  
Photoelectron Spectroscopy ◽  
High Resolution Electron Microscopy ◽  
Cross Sectional ◽  
Force Microscopy ◽  
Sapphire Substrates ◽  
Atomic Force ◽  
Resolution Electron

AbstractThe incorporation of nitrogen into sapphire substrates during nitridation was studied by xray photoelectron spectroscopy (XPS). An increase in the intensity of nitrogen 1s peak in XPS was observed upon longer nitridation. The surface morphology of the substrates was characterized by atomic force microscopy (AFM). High resolution electron microscopy (HREM) was employed for structural analysis. The cross sectional TEM showed a thin layer of AlN buried between amorphous AlNxO1−x and sapphire. This is the first direct observation of AlN on sapphire. The TEM images show a deeper penetration depth of nitrogen into a longer nitridated sapphire.

scholarly journals Atomic force microscopy of native human metaphase chromosomes in a liquid

2006 ◽  
Vol 69 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Osamu Hoshi ◽  
Masatsugu Shigeno ◽  
Tatsuo Ushiki
Keyword(s):  
Atomic Force Microscopy ◽  
Metaphase Chromosomes ◽  
Force Microscopy ◽  
Atomic Force

Robust classification of biological samples in atomic force microscopy images via multiple filtering cooperation

2017 ◽  
Vol 133 ◽  
pp. 221-233 ◽  
Author(s):  
Paola Casti ◽  
Arianna Mencattini ◽  
Innocenzo Sammarco ◽  
Sowmya Jayaraman Velappa ◽  
Gabriele Magna ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Biological Samples ◽  
Robust Classification ◽  
Force Microscopy ◽  
Atomic Force ◽  
Microscopy Images

scholarly journals Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis

2021 ◽  
Author(s):  
Liisa Lutter ◽  
Youssra Al-Hilaly ◽  
Christopher J. Serpell ◽  
Mick F. Tuite ◽  
Claude M. Wischik ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Atomic Force Microscopy ◽  
Image Analysis ◽  
Structural Analysis ◽  
Amyloid Fibrils ◽  
Structural Identification ◽  
Force Microscopy ◽  
Atomic Force ◽  
Cryo Electron Microscopy

The presence of amyloid fibrils is a hallmark of more than 50 human disorders, including neurodegenerative diseases and systemic amyloidoses. A key unresolved challenge in understanding the involvement of amyloid in disease is to explain the relationship between individual structural polymorphs of amyloid fibrils, in potentially mixed populations, and the specific pathologies with which they are associated. Although cryo-electron microscopy (cryo-EM) and solid-state nuclear magnetic resonance (ssNMR) spectroscopy methods have been successfully employed in recent years to determine the structures of amyloid fibrils with high resolution detail, they rely on ensemble averaging of fibril structures in the entire sample or significant subpopulations. Here, we report a method for structural identification of individual fibril structures imaged by atomic force microscopy (AFM) by integration of high-resolution maps of amyloid fibrils determined by cryo-EM in comparative AFM image analysis. This approach was demonstrated using the hitherto structurally unresolved amyloid fibrils formed in vitro from a fragment of tau (297-391), termed 'dGAE'. Our approach established unequivocally that dGAE amyloid fibrils bear no structural relationship to heparin-induced tau fibrils formed in vitro. Furthermore, our comparative analysis resulted in the prediction that dGAE fibrils are closely related structurally to the paired helical filaments (PHFs) isolated from Alzheimer's disease (AD) brain tissue characterised by cryo-EM. These results show the utility of individual particle structural analysis using AFM, provide a workflow of how cryo-EM data can be incorporated into AFM image analysis and facilitate an integrated structural analysis of amyloid polymorphism.

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