scholarly journals In-line three-dimensional holography of nanocrystalline objects at atomic resolution

2016 ◽  
Vol 7 (1) ◽  
Author(s):  
F.-R. Chen ◽  
D. Van Dyck ◽  
C. Kisielowski
Author(s):  
Kenneth H. Downing ◽  
Hu Meisheng ◽  
Hans-Rudolf Went ◽  
Michael A. O'Keefe

With current advances in electron microscope design, high resolution electron microscopy has become routine, and point resolutions of better than 2Å have been obtained in images of many inorganic crystals. Although this resolution is sufficient to resolve interatomic spacings, interpretation generally requires comparison of experimental images with calculations. Since the images are two-dimensional representations of projections of the full three-dimensional structure, information is invariably lost in the overlapping images of atoms at various heights. The technique of electron crystallography, in which information from several views of a crystal is combined, has been developed to obtain three-dimensional information on proteins. The resolution in images of proteins is severely limited by effects of radiation damage. In principle, atomic-resolution, 3D reconstructions should be obtainable from specimens that are resistant to damage. The most serious problem would appear to be in obtaining high-resolution images from areas that are thin enough that dynamical scattering effects can be ignored.


RSC Advances ◽  
2016 ◽  
Vol 6 (80) ◽  
pp. 76273-76279 ◽  
Author(s):  
Jaehyun Han ◽  
Jun-Young Lee ◽  
Jeongun Choe ◽  
Jong-Souk Yeo

Two-dimensional (2D) atomic crystals are very interesting materials due to their unique properties, which are significantly different than those observed in conventional three-dimensional (3D) materials.


2014 ◽  
Vol 20 (S3) ◽  
pp. 60-61
Author(s):  
Lewys Jones ◽  
Vidar T. Fauske ◽  
Katherine E. MacArthur ◽  
Antonius T. J. van Helvoort ◽  
Peter D. Nellist

2013 ◽  
Vol 88 (10) ◽  
Author(s):  
Chun Zhu ◽  
Chien-Chun Chen ◽  
Jincheng Du ◽  
Michael R. Sawaya ◽  
M. C. Scott ◽  
...  

Nature ◽  
2013 ◽  
Vol 496 (7443) ◽  
pp. 74-77 ◽  
Author(s):  
Chien-Chun Chen ◽  
Chun Zhu ◽  
Edward R. White ◽  
Chin-Yi Chiu ◽  
M. C. Scott ◽  
...  

2012 ◽  
Vol 3 ◽  
pp. 637-650 ◽  
Author(s):  
Mehmet Z Baykara ◽  
Omur E Dagdeviren ◽  
Todd C Schwendemann ◽  
Harry Mönig ◽  
Eric I Altman ◽  
...  

Noncontact atomic force microscopy (NC-AFM) is being increasingly used to measure the interaction force between an atomically sharp probe tip and surfaces of interest, as a function of the three spatial dimensions, with picometer and piconewton accuracy. Since the results of such measurements may be affected by piezo nonlinearities, thermal and electronic drift, tip asymmetries, and elastic deformation of the tip apex, these effects need to be considered during image interpretation. In this paper, we analyze their impact on the acquired data, compare different methods to record atomic-resolution surface force fields, and determine the approaches that suffer the least from the associated artifacts. The related discussion underscores the idea that since force fields recorded by using NC-AFM always reflect the properties of both the sample and the probe tip, efforts to reduce unwanted effects of the tip on recorded data are indispensable for the extraction of detailed information about the atomic-scale properties of the surface.


2018 ◽  
Author(s):  
Kok Lian Ho ◽  
Mads Gabrielsen ◽  
Poay Ling Beh ◽  
Chare Li Kueh ◽  
Qiu Xian Thong ◽  
...  

AbstractMacrobrachium rosenbergii nodavirus (MrNV) is a pathogen of freshwater prawns that poses a threat to food-security and causes significant economic losses in the aquaculture industries of many developing nations. A detailed understanding of the MrNV virion structure will inform the development of strategies to control outbreaks. The MrNV capsid has also been engineered to display heterologous antigens, thus knowledge of its atomic resolution structure will benefit efforts to develop tools based on this platform. Here we present an atomic-resolution model of the MrNV capsid protein, calculated by cryogenic electron microscopy (cryoEM) of MrNV virus-like particles (VLPs) produced in insect cells, and three-dimensional image reconstruction at 3.3 Å resolution. CryoEM of MrNV virions purified from infected freshwater prawn post-larvae yielded a 6.6 Å resolution structure confirming the biological relevance of the VLP structure.Our data revealed that unlike other known nodaviruses structures, which have been shown to assemble capsids having trimeric spikes, MrNV assembles a T=3 capsid with dimeric spikes. We also found a number of surprising similarities between the MrNV capsid structure and that of the Tombusviridae. 1. An extensive network of N-terminal arms lines the capsid interior forming long-range interactions to lace together asymmetric units. 2. The capsid shell is stabilised by three pairs of Ca2+ ions in each asymmetric unit. 3. The protruding spike domain exhibits a very similar fold to that seen in the spikes of the tombusviruses. These structural similarities raise questions concerning the correct taxonomic classification of MrNV.


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