High resolution x-ray medical sequential image acquisition and processing system based on PCI interface

2003 ◽  
Author(s):  
Dongming Lu ◽  
Qian Chen ◽  
Guohua Gu
Keyword(s):  
High Resolution ◽  
Image Acquisition ◽  
Processing System ◽  
X Ray ◽  
Sequential Image ◽  
Pci Interface

Digital imaging microscopy for molecular cytogenetics

1994 ◽  
Vol 52 ◽  
pp. 82-83
Author(s):  
J. Gray ◽  
S. Lockett ◽  
L. Mascio ◽  
J. Mullikin ◽  
D. Pinkel ◽  
...  
Keyword(s):  
High Resolution ◽  
Digital Imaging ◽  
Dynamic Range ◽  
Image Acquisition ◽  
Molecular Cytogenetics ◽  
Processing System ◽  
Frame Rate ◽  
Video Frame ◽  
Comparative Genomic ◽  
Digital Imaging Microscopy

Digital imaging microscopy is an essential tool in molecular cytogenetics. We describe here, hardware and software for sensitive multi-color image acquisition and display, gene mapping, generation ofcopy number karyotypes using comparative genomic hybridization (CGH), and correlation between genotype and histology in three dimensions.(a) QUantitative Image Processing System (QUIPS):Hardware We have developed a QUIPS that is now in routine use. This system is built around a commercial fluorescence microscope equipped with computer-controlled stage, focus and fluorescence excitation filter selection. A high resolution cooled CCD camera and a video frame rate intensified CCD (ICCD) are attached to different ports on the microscope and light is split between them. The real time images of the ICCD are continuously displayed on a monitor and are used for visual scanning and focusing. The high resolution CCD is used for image acquisition. Images from the CCD are digitized at 12 bits per pixel resulting in high dynamic range and high precision. QUIPS employs a fluorescence filter package containing a beam splitter and emission filter that pass light in bands centered at approximately 440 nm (blue), 525 nm (green) and 600 nm (red).

The DFP 9200 Digital Noise Reducer, A Real-Time High-Resolution Digital Video Processing System For X-Ray Fluoroscopy

1981 ◽  
Author(s):  
Renville H. McMann, Jr. ◽  
Stanley Baron ◽  
Stephen Kreinik ◽  
Don Epperson ◽  
Robert A. Kruger
Keyword(s):  
High Resolution ◽  
Real Time ◽  
Video Processing ◽  
Digital Video ◽  
Processing System ◽  
X Ray ◽  
Digital Video Processing

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.

High Resolution Study of Polytypism: Application to SiC and Au3 Mn

1982 ◽  
Vol 40 ◽  
pp. 540-541
Author(s):  
G. Van Tendeloo ◽  
J. Van Landuyt ◽  
S. Amelinckx
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Stacking Sequence ◽  
X Ray ◽  
Powerful Technique ◽  
Resolution Study ◽  
The Ideal

Polytypism has been studied for a number of years and a wide variety of stacking sequences has been detected and analysed. SiC is the prototype material in this respect; see e.g. Electron microscopy under high resolution conditions when combined with x-ray measurements is a very powerful technique to elucidate the correct stacking sequence or to study polytype transformations and deviations from the ideal stacking sequence.

A High Resolution Study of G.P. Zones in Aluminum - 4.2 at % Silver

1982 ◽  
Vol 40 ◽  
pp. 722-723 ◽  
Author(s):  
R. Gronsky
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
High Resolution ◽  
Computer Simulations ◽  
Structural Characteristics ◽  
X Ray Diffraction ◽  
X Ray ◽  
Transmission Electron ◽  
Resolution Study

The phenomenon of clustering in Al-Ag alloys has been extensively studied since the early work of Guinierl, wherein the pre-precipitation state was characterized as an assembly of spherical, ordered, silver-rich G.P. zones. Subsequent x-ray and TEM investigations yielded results in general agreement with this model. However, serious discrepancies were later revealed by the detailed x-ray diffraction - based computer simulations of Gragg and Cohen, i.e., the silver-rich clusters were instead octahedral in shape and fully disordered, atleast below 170°C. The object of the present investigation is to examine directly the structural characteristics of G.P. zones in Al-Ag by high resolution transmission electron microscopy.

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).

Scanning x-ray fluorescence microscopy and principal component analysis

1992 ◽  
Vol 50 (2) ◽  
pp. 1752-1753
Author(s):  
Brian Cross
Keyword(s):  
Principal Component Analysis ◽  
Fluorescence Microscopy ◽  
Spatial Resolution ◽  
High Speed ◽  
Image Acquisition ◽  
Principal Component ◽  
Fluorescence Microscope ◽  
Acquisition Rate ◽  
X Ray ◽  
Speed Up

A relatively new entry, in the field of microscopy, is the Scanning X-Ray Fluorescence Microscope (SXRFM). Using this type of instrument (e.g. Kevex Omicron X-ray Microprobe), one can obtain multiple elemental x-ray images, from the analysis of materials which show heterogeneity. The SXRFM obtains images by collimating an x-ray beam (e.g. 100 μm diameter), and then scanning the sample with a high-speed x-y stage. To speed up the image acquisition, data is acquired "on-the-fly" by slew-scanning the stage along the x-axis, like a TV or SEM scan. To reduce the overhead from "fly-back," the images can be acquired by bi-directional scanning of the x-axis. This results in very little overhead with the re-positioning of the sample stage. The image acquisition rate is dominated by the x-ray acquisition rate. Therefore, the total x-ray image acquisition rate, using the SXRFM, is very comparable to an SEM. Although the x-ray spatial resolution of the SXRFM is worse than an SEM (say 100 vs. 2 μm), there are several other advantages.

Scanning Electron Microscopy and x-ray analysis of microparticles and early hydration effects

1995 ◽  
Vol 53 ◽  
pp. 692-693
Author(s):  
Yun Lu ◽  
David C. Joy
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
High Resolution ◽  
Morphological Development ◽  
Early Hydration ◽  
X Ray ◽  
Blended Cements ◽  
Powder Particles ◽  
Chemical Wastes ◽  
Scanning Electron

High resolution scanning electron microscopy (SEM) and energy dispersive x-ray analysis (EDXA) were performed to investigate microparticles in blended cements and their hydration products containing sodium-rich chemical wastes. The physical appearance of powder particles and the morphological development at different hydration stages were characterized by using high resolution SEM Hitachi S-900 and by SEM S-800 with a EDX spectrometer. Microparticles were dispersed on the sample holder and glued by 1% palomino solution. Hydrated bulk samples were dehydrated by acetone and mounted on the holder by silver paste. Both fracture surfaces and flat cutting sections of hydrating samples were prepared and examined. Some specimens were coated with an 3 nm thick Au-Pd or Cr layer to provide good conducting surfaces. For high resolution SEM S-900 observations the accelerating voltage of electrons was 1-2 KeV to protect the electron charging. Microchemical analyses were carried out by S800/EDS equipped with a LINK detector of take-off angle =40°.

Tubulin structure at intermediate resolution

1995 ◽  
Vol 53 ◽  
pp. 852-853
Author(s):  
K. H. Downing ◽  
S. G. Wolf ◽  
E. Nogales
Keyword(s):  
High Resolution ◽  
Structural Data ◽  
Therapeutic Drug ◽  
Zinc Ions ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
X Ray ◽  
Negative Stain ◽  
Functional Mechanisms ◽  
Tubulin Structure

Microtubules are involved in a host of critical cell activities, many of which involve transport of organelles through the cell. Different sets of microtubules appear to form during the cell cycle for different functions. Knowledge of the structure of tubulin will be necessary in order to understand the various functional mechanisms of microtubule assemble, disassembly, and interaction with other molecules, but tubulin has so far resisted crystallization for x-ray diffraction studies. Fortuitously, in the presence of zinc ions, tubulin also forms two-dimensional, crystalline sheets that are ideally suited for study by electron microscopy. We have refined procedures for forming the sheets and preparing them for EM, and have been able to obtain high-resolution structural data that sheds light on the formation and stabilization of microtubules, and even the interaction with a therapeutic drug.Tubulin sheets had been extensively studied in negative stain, demonstrating that the same protofilament structure was formed in the sheets and microtubules. For high resolution studies, we have found that the sheets embedded in either glucose or tannin diffract to around 3 Å.

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