Analysis of composition changes across the Si/SiOx interface using fresnel fringe contrast analysis

1987 ◽  
Vol 105 ◽  
Author(s):  
Frances M. Ross ◽  
W. M. Stobbs
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Structural Changes ◽  
High Resolution Electron Microscopy ◽  
Atomic Resolution ◽  
Fringe Contrast ◽  
Resolution Electron ◽  
Contrast Analysis ◽  
Composition Changes

AbstractFresnel fringe contrast analysis and high resolution electron microscopy are used in conjunction to measure compositional and structural changes across the Si/SiOx interface with atomic resolution.

Atomic-Resolution Electron Microscopy of TiB2 Precipitates in an Industrial TiAl Alloy

1996 ◽  
Vol 466 ◽  
Author(s):  
B. J. Inkson ◽  
G. Möbus ◽  
M. Rühle
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Tial Alloy ◽  
High Resolution Electron Microscopy ◽  
Atomic Resolution ◽  
Resolution Electron ◽  
B2 Phase ◽  
Relationship Of ◽  
Orientational Relationship

ABSTRACTTiB2 nano-lamellae, grown in-situ within a TiAl intermetallic melt, have been examined by high resolution electron microscopy. The use of the Stuttgart ARM enables Ti and B columns to be distinguished in the HREM images. Examination of the internal structure of the T1B2 platelets reveals extensive prismatic faulting on {1010}TiB2, {0110}TiB2 and {1100}TiB2 planes. Externally, the TiB2 platelets exhibit an orientational relationship {1010}TiB2 // {001}B2 and [0001]TiB2 // <010>B2 with interleaving platelets of B2-phase, with the predominating interface planes being {1010}TiB2 // {001}B2. The minor facets of the TiB2 platelets are [0001]TiB2 // <010>B2. {0110}TiB2 and {1100}TiB2, with the latter two facets showing no relationship with the interleaving B2-phase. No preferred orientation relationship of the TiB2 with the surrounding γ-TiAl and α2-Ti3Al phases is observed.

Sectorized crystallization of higher n-alkanes: A high resolution search for oblique chain packing

1989 ◽  
Vol 47 ◽  
pp. 344-345
Author(s):  
D. L. Dorset ◽  
J. C. Wittmann ◽  
B. Lotz ◽  
C. H. McConnell ◽  
J. R. Fryer ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Infinite Chain ◽  
Bright Field ◽  
Fringe Contrast ◽  
Chain Packing ◽  
Resolution Electron ◽  
Fritz Haber

Although it was once thought that a major distinction between paraffin and polyethylene lozenge crystals was the sectorization of the latter due to polarization of chain fold surfaces, a recent study has shown that n-paraffins longer than C44H90, but with unfolded chains, also crystallize as sectorized lozenges (Fig. 1) with bright field fringes running along <130> compared to the <130> direction in polyethylene. High resolution electron microscopy and microdiffraction of corrugated polyethylene lozenges, furthermore, have shown that, for the infinite chain folded polymer, these fringes correspond to local oblique chain packings. Although shadowing with C-Pt indicates that the sectorized paraffin lozenges are not corrugated like polyethylene, it was thought that chain obliquity, nevertheless, should also be the cause of the Bragg fringe contrast in Fig. 1.An attempt was made to visualize the detail directly using the SULEIKA cryomicroscope at the Fritz Haber Institute in Berlin, given our previous success in obtaining 2.5Å resolution images of the C44H90 chain packing.

Defects and Metal Particles in Zeolites Studied with High Resolution Electron Microscopy

1990 ◽  
Vol 183 ◽  
Author(s):  
H. W. Zandbergen ◽  
D. van Dyck
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Structural Changes ◽  
Zeolite Y ◽  
High Resolution Electron Microscopy ◽  
Metal Particles ◽  
Zeolite L ◽  
Zeolite Β ◽  
Resolution Electron

AbstractA number of examples of high resolution electron microscopy on defects and metal particles in zeolites is given: defects in Zeolite Y and Zeolite β, metal particles in ZSM-5, and structural changes due to reactions in Zeolite L and Zeolite Y.

Characterization of Ultrathin Doping Layers in Semiconductors

1997 ◽  
Vol 3 (4) ◽  
pp. 352-363 ◽  
Author(s):  
C.P. Liu ◽  
R.E. Dunin-Borkowski ◽  
C.B. Boothroyd ◽  
P.D. Brown ◽  
C.J. Humphreys
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Dark Field ◽  
High Angle ◽  
Compositional Profile ◽  
Resolution Electron ◽  
Annular Dark Field ◽  
Contrast Analysis

Abstract: The compositional profile of a narrow layer of InAsxPl−x in InP has been determined using energy-filtered Fresnel contrast analysis, high-resolution electron microscopy (HREM), and high-angle annular dark-field (HAADF) imaging. The consistency of the results obtained using the three techniques is discussed, and conclusions are drawn both about the validity of interpreting the magnitude of Fresnel contrast data quantitatively and about the degree to which high-angle annular dark-field images of such materials are affected by inelastic scattering and strain.

High-resolution electron microscopy of amorphization of Cu4 Ti3

1986 ◽  
Vol 1 (5) ◽  
pp. 617-628 ◽  
Author(s):  
D.E. Luzzi ◽  
M. Meshii
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Intermetallic Compound ◽  
Driving Force ◽  
High Resolution Electron Microscopy ◽  
Amorphous Structure ◽  
Crystalline Region ◽  
Fringe Contrast ◽  
Chemical Order ◽  
Resolution Electron

The electron irradiation-induced, crystalline-to-amorphous transition was studied in the intermetallic compound Cu4Ti3 by high-resolution electron microscopy. Using highresolution maps from the crystalline region into the amorphized region, the amorphization process and the amorphous structure were examined. The extent of chemical order in crystalline regions just prior to amorphization was studied by simultaneously imaging superlattice and fundamental lattice fringe contrast. The chemical order continuously decreased in these regions but faint superlattice contrast was recognized as long as the crystalline feature remained on the image, supporting the theory that chemical disordering is the major driving force for amorphization. The amorphization process appears to be evolutionary, leading to a nanocrystalline type of amorphous structure. A model of the amorphization process is proposed based on the present results and those from previous studies.

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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