Molecular imaging of Organo-Calcium salts by High Resolution Electron Microscopy and Image Processing

Author(s):  
G. Miller ◽  
J.R. Fryer ◽  
W. Kunath ◽  
K. Weiss

Unfortunatly Wolfgang Kunath died January 1990High resolution electron microscopy and image processing are being used to determine the molecular packing within the crystal unit cell of the, organic-azo calcium salt. Due to the beam sensitive nature of the organic moiety which contains both aromatic and and aliphatic components, low dose techniques were used. This concisted of, searching the sample in the diffraction mode to find single crystals exibiting point like reflection to at least .2nm resolution, (fig. 1). Focusing and astigmatism correction was performed by moving the beam of the crystal (off axis). The beam was then moved on axis and a series of four, 10 e/A images taken, (fig. 2). Images were primarily recorded using an on line T.V. recording device. These images were then available for processing using the Semper image processing system. Two crystal orientations were found. Type 1 consisted of thin plate like crystals up to 5um diameter and generally 10nm to 20nm thick. Type 2 were thicker crystals with a 3.2nm lattice spacing. The power specrta of the first low dose images were calculated to asses the quality of the of the structural information present. For the type 1 crystal the power spectrum had to show at least second order reflections in two directions ( fig. 3 ). Type 2 crystals showed the 3.2nm reflection often down to the fith order. These crystals also showed parallel side bands corresponding to a d-spacing of about .8nm. With these results the unit cell was found to be tetragonal with a= .78nm b= 3.2nm c= .78nm. In accordance with the diffraction patterns exibited.

Author(s):  
W. H. Wu ◽  
R. M. Glaeser

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.


Author(s):  
M. Pan

It has been known for many years that materials such as zeolites, polymers, and biological specimens have crystalline structures that are vulnerable to electron beam irradiation. This radiation damage severely restrains the use of high resolution electron microscopy (HREM). As a result, structural characterization of these materials using HREM techniques becomes difficult and challenging. The emergence of slow-scan CCD cameras in recent years has made it possible to record high resolution (∽2Å) structural images with low beam intensity before any apparent structural damage occurs. Among the many ideal properties of slow-scan CCD cameras, the low readout noise and digital recording allow for low-dose HREM to be carried out in an efficient and quantitative way. For example, the image quality (or resolution) can be readily evaluated on-line at the microscope and this information can then be used to optimize the operating conditions, thus ensuring that high quality images are recorded. Since slow-scan CCD cameras output (undistorted) digital data within the large dynamic range (103-104), they are ideal for quantitative electron diffraction and microscopy.


1988 ◽  
Vol 107 (2) ◽  
pp. 521-530 ◽  
Author(s):  
W. Coene ◽  
A. F. de Jong ◽  
D. van Dyck ◽  
G. van Tendeloo ◽  
J. van Landuyt

A previously described solid solution in the system Bi 2 O 3 -Nb 2 O 5 based on the δ-Bi 2 O 3 structure has been reinvestigated by electron diffraction and high resolution electron microscopy. Four distinct phases have been found, all of which are based upon defect fluorite structures, and the structural principles of the phase with the greatest compositional range have been elucidated. This involves an adaption of elements of the pyrochlore structure with an ordering of niobium-oxygen octahedra into groups lying on the {111} planes of an enlarged cubic unit cell, separated by a matrix of δ-Bi 2 O 3 structure.


1997 ◽  
Vol 3 (S2) ◽  
pp. 441-442
Author(s):  
P.A. Crozier ◽  
I.Y. Chan ◽  
C.Y. Chen ◽  
L.W. Finger ◽  
R.C. Medrud ◽  
...  

Low-dose high resolution electron microscopy (HREM) is a useful technique for elucidating the structure of zeolites. In recent years a number of zeolite structures have been solved using combinations of different characterization techniques including adsorption measurements, powder x-ray diffraction and low-dose high resolution electron microscopy (for example see ref. 2). We have used these techniques to study the structure of a novel zeolite material. However, great care must be exercised when interpreting data from these techniques in terms of crystal structural units. In this particular case, the structure was recently determined using single crystal x-ray diffraction and showed some surprises.Details of the synthesis of this zeolite are given elsewhere. The high adsorption capacity suggested that this zeolite possessed two interpenetrating channels (either a 10 and a 12 ring or two 12 ring channels). X-ray powder diffraction showed the material to be monoclinic with a= 18.5Å, b= 13.4 Å, c= 7.6 Å β = 101.5°).


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