scholarly journals Embedded Nanoparticle Analysis using Atom Probe Tomography and High-Resolution Electron Microscopy

2011 ◽  
Vol 17 (S2) ◽  
pp. 760-761 ◽  
Author(s):  
S Kuchibhatla ◽  
V Shutthanandan ◽  
B Arey ◽  
L Kovarik ◽  
C Wang ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Atom Probe Tomography ◽  
High Resolution Electron Microscopy ◽  
Atom Probe ◽  
Resolution Electron

Extended abstract of a paper presented at Microscopy and Microanalysis 2011 in Nashville, Tennessee, USA, August 7–August 11, 2011.

3D Atom Probe Tomography and High Resolution Electron Microscopy of Immiscible Copper/Niobium Metallic Multilayers

2007 ◽  
Vol 13 (S02) ◽  
Author(s):  
A Genç ◽  
Ohio State University ◽  
University of North Texas ◽  
Ohio State University ◽  
University of North Texas
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Atom Probe Tomography ◽  
High Resolution Electron Microscopy ◽  
Atom Probe ◽  
Metallic Multilayers ◽  
Resolution Electron

Fabrication and characterization - by High Resolution Electron Microscopy and atom probe microanalysis - of Co-based metallic multilayer films

1990 ◽  
Vol 48 (4) ◽  
pp. 772-773
Author(s):  
Amanda K. Petford-Long ◽  
A. Cerezo ◽  
M.G. Hetherington
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Atom Probe ◽  
Multilayer Films ◽  
Interface Roughness ◽  
Probe Field ◽  
Resolution Electron ◽  
Potential Applications ◽  
Field Ion Microscope

The fabrication of multilayer films (MLF) with layer thicknesses down to one monolayer has led to the development of materials with unique properties not found in bulk materials. The properties of interest depend critically on the structure and composition of the films, with the interfacial regions between the layers being of particular importance. There are a number of magnetic MLF systems based on Co, several of which have potential applications as perpendicular magnetic (e.g Co/Cr) or magneto-optic (e.g. Co/Pt) recording media. Of particular concern are the effects of parameters such as crystallographic texture and interface roughness, which are determined by the fabrication conditions, on magnetic properties and structure.In this study we have fabricated Co-based MLF by UHV thermal evaporation in the prechamber of an atom probe field-ion microscope (AP). The multilayers were deposited simultaneously onto cobalt field-ion specimens (for AP and position-sensitive atom probe (POSAP) microanalysis without exposure to atmosphere) and onto the flat (001) surface of oxidised silicon wafers (for subsequent study in cross-section using high-resolution electron microscopy (HREM) in a JEOL 4000EX. Deposi-tion was from W filaments loaded with material in the form of wire (Co, Fe, Ni, Pt and Au) or flakes (Cr). The base pressure in the chamber was around 8×10−8 torr during deposition with a typical deposition rate of 0.05 - 0.2nm/s.

Atom Probe and Hrem Characterization of Transition Metal Multilayers.

1990 ◽  
Vol 187 ◽  
Author(s):  
A. Cerezo ◽  
M.G. Hetherington ◽  
A.J.K. Petford-Long
Keyword(s):  
Crystal Structure ◽  
Electron Microscopy ◽  
High Resolution ◽  
Transition Metal ◽  
High Resolution Electron Microscopy ◽  
Atom Probe ◽  
Complementary Information ◽  
Resolution Electron ◽  
Position Sensitive

AbstractThe direct measurement of the composition variations in transition metal multilayers has been carried out using the atom-probe and the position sensitive atom-probe (POSAP). The atom-probe and POSAP do not have sufficient resolution to determine the crystal structure and this complementary information has been obtained using high resolution electron microscopy.

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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