Dynamical diffraction effects on high-resolution electron microscopy of ordered alloys

1988 ◽  
Vol 44 (6) ◽  
pp. 954-960 ◽  
Author(s):  
D. Shindo ◽  
M. Hirabayashi
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Dynamical Diffraction ◽  
Resolution Electron ◽  
Ordered Alloys ◽  
Diffraction Effects

Periodic Extension in Optical Diffraction Analysis

1982 ◽  
Vol 40 ◽  
pp. 428-429
Author(s):  
R. Gronsky ◽  
C.S. Murty
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Considerable Increase ◽  
High Resolution Electron Microscopy ◽  
Optical Diffraction ◽  
Diffraction Spectrum ◽  
Optical Bench ◽  
Instrumental Performance ◽  
Resolution Electron ◽  
Diffraction Effects

Although the more traditional applications of optical diffractograms in high resolution electron microscopy are related to determining instrumental performance, a significant advantage can also be achieved with this technique in the analysis of fine microstructural detail. Optical microdiffraction utilizes a field-limiting aperture in the optical bench system to selectively obtain the diffraction spectrum of specific segments of high resolution negatives, with a considerable increase in spatial resolution. Unfortunately the diffraction effects from the sampling aperture itself often interfere with the interpretation of results

Structure analyses of long range ordered alloys by high voltage, high resolution electron microscopy

Micron (1969) ◽  
1980 ◽  
Vol 11 (3-4) ◽  
pp. 235-240 ◽  
Author(s):  
O. Terasaki ◽  
D. Watanabe ◽  
K. Hiraga ◽  
D. Shindo ◽  
M. Hirabayashi
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Long Range ◽  
High Voltage ◽  
High Resolution Electron Microscopy ◽  
Resolution Electron ◽  
Ordered Alloys

Structural analysis of the surface-layer protein of spirillum serpens by high-resolution electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 738-739
Author(s):  
W. H. Wu ◽  
R. M. Glaeser
Keyword(s):  
Electron Microscopy ◽  
Surface Layer ◽  
Structural Analysis ◽  
High Resolution ◽  
Low Dose ◽  
High Resolution Electron Microscopy ◽  
Optical Diffraction ◽  
Surface Layer Protein ◽  
Morphological Unit ◽  
Resolution Electron

Spirillum serpens possesses a surface layer protein which exhibits a regular hexagonal packing of the morphological subunits. A morphological model of the structure of the protein has been proposed at a resolution of about 25 Å, in which the morphological unit might be described as having the appearance of a flared-out, hollow cylinder with six ÅspokesÅ at the flared end. In order to understand the detailed association of the macromolecules, it is necessary to do a high resolution structural analysis. Large, single layered arrays of the surface layer protein have been obtained for this purpose by means of extensive heating in high CaCl2, a procedure derived from that of Buckmire and Murray. Low dose, low temperature electron microscopy has been applied to the large arrays.As a first step, the samples were negatively stained with neutralized phosphotungstic acid, and the specimens were imaged at 40,000 magnification by use of a high resolution cold stage on a JE0L 100B. Low dose images were recorded with exposures of 7-9 electrons/Å2. The micrographs obtained (Fig. 1) were examined by use of optical diffraction (Fig. 2) to tell what areas were especially well ordered.

Electron microscopy of rabbit FC crystals

1983 ◽  
Vol 41 ◽  
pp. 730-731
Author(s):  
Robert A. Grant ◽  
Laura L. Degn ◽  
Wah Chiu ◽  
John Robinson
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Molecular Replacement ◽  
X Ray ◽  
X Ray Crystallography ◽  
Resolution Electron ◽  
Replacement Technique ◽  
Hydrated Crystal ◽  
Molecular Structure Analysis

Proteolytic digestion of the immunoglobulin IgG with papain cleaves the molecule into an antigen binding fragment, Fab, and a compliment binding fragment, Fc. Structures of intact immunoglobulin, Fab and Fc from various sources have been solved by X-ray crystallography. Rabbit Fc can be crystallized as thin platelets suitable for high resolution electron microscopy. The structure of rabbit Fc can be expected to be similar to the known structure of human Fc, making it an ideal specimen for comparing the X-ray and electron crystallographic techniques and for the application of the molecular replacement technique to electron crystallography. Thin protein crystals embedded in ice diffract to high resolution. A low resolution image of a frozen, hydrated crystal can be expected to have a better contrast than a glucose embedded crystal due to the larger density difference between protein and ice compared to protein and glucose. For these reasons we are using an ice embedding technique to prepare the rabbit Fc crystals for molecular structure analysis by electron microscopy.

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