Effect of Atomic Level Width on Ge(Li) X-ray Spectra

1974 ◽  
Vol 28 (5) ◽  
pp. 445-448
Author(s):  
B. P. Pathak ◽  
S. K. Makherjee

The shapes of x-ray and γ-ray peaks have been studied with the use of a high resolution Ge(Li) spectrometer. The Kα x-ray peaks of high Z elements have been found to exhibit larger width compared to the width of γ-ray peaks of same energy. This excess width has been assigned to the natural energy width of characteristic x-ray lines. An analytical study of the variation of the observed width with the natural width of the incident radiation has been made. The computed results are in excellent agreement with the experimental observation.

1996 ◽  
Vol 251 (3-4) ◽  
pp. 219-222 ◽  
Author(s):  
Takayuki Kumada ◽  
Hirohisa Inagaki ◽  
Takao Nagasawa ◽  
Yasuyuki Aratono ◽  
Tetsuo Miyazaki

Author(s):  
Nobuo Tanaka ◽  
Ken-ichi Ohshima ◽  
Jinpei Harada ◽  
J.M. Cowley

Observation of short range ordered (SRO) state in disordered binary alloys is the interesting topic in the point of order-disorder transition. The observation and analysis have been made with X-ray and neutron diffraction techniques which can give the SRO-parameters. These techniques, however, give only the information of an averaged structure. The ordering process is localized, so direct observations in atomic level by high resolution electron microscopy is needed for the detailed analysis.In the present study, disordered Au4Mn alloys were investigated with high resolution electron microscopy for the analysis of the origin of the characteristic SRO diffuse scattering (Fig. 1). The material was prepared by quenching and thinned by electrolytic polishing for microscopic observations. The specimen was observed along <120> direction by JEOL-200CX electron microscope (E=200keV).


1969 ◽  
Vol 13 ◽  
pp. 390-405 ◽  
Author(s):  
Ragnar Nordberg

The results reviewed in this article were obtained by means of the ESCA technique at the Institute of Physics, University of Uppsala, Uppsala, Sweden and at the Department of Physics, Vanderbilt University, Nashville, Tennessee, USA.The ESCA technique is basically the study of induced emission of photo and Auger electrons from a sample irradiated with x-rays. If the incident radiation is monochromatic (e.g. an x-ray emission line) the spectrum of these electrons gives precise information about the energy states of the electrons in the sample. To extract this information, high resolution electron spectroscopy is necessary. Instruments for such spectroscopy have therefore been extensively developed during the last decade.


1976 ◽  
Vol 54 (2) ◽  
pp. 197-204 ◽  
Author(s):  
P. Sen ◽  
M. Kingman ◽  
H. Bakhru ◽  
N. Cue

The decay of 146Gd to levels of 146Eu has been studied using high resolution X-ray and γ-ray detectors. γ–γ directional correlation studies, using X and γ-ray Ge(Li) detectors, were made to assign the spins of the low lying states in 146Eu. γ–γ coincidence experiments with two Ge(Li) detectors and between Eu X rays and γ rays were performed to pin down the levels of 146Eu. On the basis of these measurements, Jπ of 4−, 3−, 2−, and 1− have been assigned respectively to the ground, 115.66, 230.51, and 385.11 keV states in 146Eu. More accurate evaluation of the E2 admixtures in the M1 transitions, 114.85, 115.66, and 154.60 keV, have been obtained. Based on the above results a tentative level scheme for 146Eu has been proposed.


Author(s):  
Robert A. Grant ◽  
Laura L. Degn ◽  
Wah Chiu ◽  
John Robinson

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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