Digital Processing of STEM Images

1981 ◽  
Vol 39 ◽  
pp. 236-237
Author(s):  
A. V. Crewe ◽  
M. Ohtsuki
Keyword(s):  
High Resolution ◽  
Low Dose ◽  
Assembly Language ◽  
Processing System ◽  
Principal Component ◽  
Digital Processing ◽  
Image Analysis System ◽  
Black And White ◽  
Analysis System ◽  
Dose Imaging

We have assembled an image processing system for use with our high resolution STEM for the particular purpose of working with low dose images of biological specimens. The system is quite flexible, however, and can be used for a wide variety of images.The original images are stored on magnetic tape at the microscope using the digitized signals from the detectors. For low dose imaging, these are “first scan” exposures using an automatic montage system. One Nova minicomputer and one tape drive are dedicated to this task.The principal component of the image analysis system is a Lexidata 3400 frame store memory. This memory is arranged in a 640 x 512 x 16 bit configuration. Images are displayed simultaneously on two high resolution monitors, one color and one black and white. Interaction with the memory is obtained using a Nova 4 (32K) computer and a trackball and switch unit provided by Lexidata.The language used is BASIC and uses a variety of assembly language Calls, some provided by Lexidata, but the majority written by students (D. Kopf and N. Townes).

Computer averaging of lattice images of poly-4-methyl-pentene-1 (P4mp1): Noise created artifacts

1987 ◽  
Vol 45 ◽  
pp. 388-389
Author(s):  
P. Pradère ◽  
J.F. Revol ◽  
R. St. John Manley
Keyword(s):  
Low Dose ◽  
Polymer Concentration ◽  
Processing System ◽  
Limiting Factor ◽  
Dilute Solution ◽  
New Techniques ◽  
Dose Unit ◽  
Lattice Images ◽  
Dose Imaging ◽  
Imaging Conditions

Although radiation damage is the limiting factor in HREM of polymers, new techniques based on low dose imaging at low magnification have permitted lattice images to be obtained from very radiation sensitive polymers such as polyethylene (PE). This paper describes the computer averaging of P4MP1 lattice images. P4MP1 is even more sensitive than PE (total end point dose of 27 C m-2 as compared to 100 C m-2 for PE at 120 kV). It does, however, have the advantage of forming flat crystals from dilute solution and no change in d-spacings is observed during irradiation.Crystals of P4MP1 were grown at 60°C in xylene (polymer concentration 0.05%). Electron microscopy was performed with a Philips EM 400 T microscope equipped with a Low Dose Unit and operated at 120 kV. Imaging conditions were the same as already described elsewhere. Enlarged micrographs were digitized and processed with the Spider image processing system.

Coronary CT angiography in patients with atrial fibrillation: Standard-dose and low-dose imaging with a high-resolution whole-heart CT scanner

2018 ◽  
Vol 28 (8) ◽  
pp. 3432-3440 ◽  
Author(s):  
Anna Matveeva ◽  
Rainer R. Schmitt ◽  
Karoline Edtinger ◽  
Matthias Wagner ◽  
Sebastian Kerber ◽  
...  
Keyword(s):  
Atrial Fibrillation ◽  
High Resolution ◽  
Ct Angiography ◽  
Coronary Ct Angiography ◽  
Low Dose ◽  
Standard Dose ◽  
Ct Scanner ◽  
Coronary Ct ◽  
Whole Heart ◽  
Dose Imaging

High Resolution Microscopy of Multi-Layered Biological Crystals

1982 ◽  
Vol 40 ◽  
pp. 80-83
Author(s):  
H.A. Cohen ◽  
T.W. Jeng ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Low Dose ◽  
Three Dimensional ◽  
Data Interpretation ◽  
Two Dimensional ◽  
Biological Objects ◽  
Density Maps ◽  
Density Map ◽  
Complex Crystal ◽  
High Resolution Microscopy

This tutorial will discuss the methodology of low dose electron diffraction and imaging of crystalline biological objects, the problems of data interpretation for two-dimensional projected density maps of glucose embedded protein crystals, the factors to be considered in combining tilt data from three-dimensional crystals, and finally, the prospects of achieving a high resolution three-dimensional density map of a biological crystal. This methodology will be illustrated using two proteins under investigation in our laboratory, the T4 DNA helix destabilizing protein gp32*I and the crotoxin complex crystal.

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.

Superior 2X2 Slides

1975 ◽  
Vol 33 ◽  
pp. 158-159
Author(s):  
Harry Schaefer ◽  
Bruce Wetzel
Keyword(s):  
New York ◽  
High Resolution ◽  
Black And White ◽  
Fine Grain ◽  
White Film

High resolution 24mm X 36mm positive transparencies can be made from original black and white negatives produced by SEM, TEM, and photomicrography with ease, convenience, and little expense. The resulting 2in X 2in slides are superior to 3¼in X 4in lantern slides for storage, transport, and sturdiness, and projection equipment is more readily available. By mating a 35mm camera directly to an enlarger lens board (Fig. 1), one combines many advantages of both. The negative is positioned and illuminated with the enlarger and then focussed and photographed with the camera on a fine grain black and white film.Specifically, a Durst Laborator 138 S 5in by 7in enlarger with 240/200 condensers and a 500 watt Opale bulb (Ehrenreich Photo-Optical Industries, Inc., New York, NY) is rotated to the horizontal and adjusted for comfortable eye level viewing.

Chemical Classification and Particle Sizing of Foundry Sands

1985 ◽  
Vol 43 ◽  
pp. 388-389
Author(s):  
D.S. DeMiglio
Keyword(s):  
Image Analysis ◽  
Energy Dispersive Spectrometer ◽  
Image Analysis System ◽  
Representative Sampling ◽  
Foundry Sands ◽  
Large Atomic Number ◽  
Backscattered Electron ◽  
Sand Particles ◽  
Analysis System ◽  
Reclamation System

Much progress has been made in recent years towards the development of closed-loop foundry sand reclamation systems. However, virtually all work to date has determined the effectiveness of these systems to remove surface clay and metal oxide scales by a qualitative inspection of a representative sampling of sand particles. In this investigation, particles from a series of foundry sands were sized and chemically classified by a Lemont image analysis system (which was interfaced with an SEM and an X-ray energy dispersive spectrometer) in order to statistically document the effectiveness of a reclamation system developed by The Pangborn Company - a subsidiary of SOHIO.The following samples were submitted: unreclaimed sand; calcined sand; calcined & mechanically scrubbed sand and unused sand. Prior to analysis, each sample was sprinkled onto a carbon mount and coated with an evaporated film of carbon. A backscattered electron photomicrograph of a field of scale-covered particles is shown in Figure 1. Due to a large atomic number difference between sand particles and the carbon mount, the backscattered electron signal was used for image analysis since it had a uniform contrast over the shape of each particle.

Automated high-resolution microscopy: the approaches so far

1987 ◽  
Vol 45 ◽  
pp. 58-61
Author(s):  
W. O. Saxton
Keyword(s):  
High Resolution ◽  
Early Stage ◽  
Automatic Recording ◽  
Microprocessor Control ◽  
Alternative Systems ◽  
Electron Image ◽  
Complete Automation ◽  
Analysis System ◽  
High Resolution Microscopy

Recent commercial microscopes with internal microprocessor control of all major functions have already demonstrated some of the benefits anticipated from such systems, such as continuous magnification, rotation-free diffraction and magnification, automatic recording of mutually registered focal series, and fewer control knobs. Complete automation of the focusing, stigmating and alignment of a high resolution microscope, allowing focal series to be recorded at preselected focus values as well, is still imminent rather than accomplished, however; some kind of image pick-up and analysis system, fed with the electron image via a TV camera, is clearly essential for this, but several alternative systems and algorithms are still being explored. This paper reviews the options critically in turn, and stresses the need to consider alignment and focusing at an early stage, and not merely as an optional extension to a basic proposal.

Quantitative nano-characterization of heterogeneous catalysts

1995 ◽  
Vol 53 ◽  
pp. 398-399
Author(s):  
P.A. Crozier ◽  
M. Pan
Keyword(s):  
Heterogeneous Catalysts ◽  
Low Dose ◽  
Imaging Techniques ◽  
Structural Features ◽  
Catalyst Characterization ◽  
New Developments ◽  
Double Phase ◽  
Phase Systems ◽  
Dose Imaging

Heterogeneous catalysts can be of varying complexity ranging from single or double phase systems to complicated mixtures of metals and oxides with additives to help promote chemical reactions, extend the life of the catalysts, prevent poisoning etc. Although catalysis occurs on the surface of most systems, detailed descriptions of the microstructure and chemistry of catalysts can be helpful for developing an understanding of the mechanism by which a catalyst facilitates a reaction. Recent years have seen continued development and improvement of various TEM, STEM and AEM techniques for yielding information on the structure and chemistry of catalysts on the nanometer scale. Here we review some quantitative approaches to catalyst characterization that have resulted from new developments in instrumentation.HREM has been used to examine structural features of catalysts often by employing profile imaging techniques to study atomic details on the surface. Digital recording techniques employing slow-scan CCD cameras have facilitated the use of low-dose imaging in zeolite structure analysis and electron crystallography. Fig. la shows a low-dose image from SSZ-33 zeolite revealing the presence of a stacking fault.

Slow-scan CCD cameras and low-dose High-Resolution Electron Microscopy: Direct and quantitative

1994 ◽  
Vol 52 ◽  
pp. 412-413
Author(s):  
M. Pan
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Structural Damage ◽  
Low Dose ◽  
Dynamic Range ◽  
High Resolution Electron Microscopy ◽  
Operating Conditions ◽  
Digital Data ◽  
Ccd Cameras ◽  
Resolution Electron

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.

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