Structure Determination of Tilt Boundaries in Gold by High Resolution Electron Microscopy

1986 ◽  
Vol 82 ◽  
Author(s):  
William Krakow ◽  
David A. Smith

ABSTRACTA number of tilt grain boundaries prepared from evaporated gold thin films have been investigated by high resolution transmission microscopy. When the grain boundary is parallel to the electron beam and the beam is parallel to a low index rotation axis such as [110] or [001]it is possible to identify atomic positions at the cores of these boundaries as demonstrated here by a Σ = 3 70.5°/[110], (112) growth twin. In many cases it is not possible to make a full atomistic structure determination because the specimen does not have translational periodicity in the beam direction. This may be because the boundary plane is not parallel to the beam or the specimen contains dislocations which have a component of Burgers vector parallel to the beam. Examples are given of various low angle boundary structures in goldwhere there are complications because of the three dimensional nature of their structure.




ChemInform ◽  
2010 ◽  
Vol 29 (30) ◽  
pp. no-no
Author(s):  
A. CARLSSON ◽  
T. OKU ◽  
J.-O. BOVIN ◽  
R. WALLENBERG ◽  
J.-O. MALM ◽  
...  


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.



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