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.

High Resolution Electron Microscopic Study of the Growth of Denser Phases on Zeolite Y and Zeolite L.

1987 ◽  
Vol 111 ◽  
Author(s):  
H. W. Zandbergen
Keyword(s):  
High Resolution ◽  
Local Structure ◽  
Zeolite Y ◽  
High Resolution Electron Microscopy ◽  
Electron Microscopic ◽  
Detailed Characterization ◽  
Zeolite L ◽  
Resolution Electron ◽  
Materials Research

AbstractHigh resolution electron microscopy (HREM) is a powerful tool in materials research. This is especially true in the study of zeolites because most of the questions concerning the properties of zeolites require a detailed characterization of the local structure [1]. The potential of HREM is illustrated with studies on the growth of denser phases on Zeolite Y and Zeolite L.

Surface Structure of Zeolite L Studied by High-Resolution Electron Microscopy

1998 ◽  
Vol 10 (3) ◽  
pp. 688-691 ◽  
Author(s):  
Tetsu Ohsuna ◽  
Yasuyoshi Horikawa ◽  
Kenji Hiraga ◽  
Osamu Terasaki
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Surface Structure ◽  
High Resolution Electron Microscopy ◽  
Zeolite L ◽  
Resolution Electron

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.

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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