High-Resolution X-ray Photoelectron Spectra of Organosulfur Monolayers on Au(111):  S(2p) Spectral Dependence on Molecular Species

Langmuir ◽  
1999 ◽  
Vol 15 (20) ◽  
pp. 6799-6806 ◽  
Author(s):  
Takao Ishida ◽  
Nami Choi ◽  
Wataru Mizutani ◽  
Hiroshi Tokumoto ◽  
Isao Kojima ◽  
...  
1993 ◽  
Vol 68 (3) ◽  
pp. 291-298 ◽  
Author(s):  
Th. Gross ◽  
A. Lippitz ◽  
W.E.S. Unger ◽  
Ch. Wöll ◽  
G. Hähner ◽  
...  

2004 ◽  
Vol 121 (20) ◽  
pp. 10260-10267 ◽  
Author(s):  
A. Schöll ◽  
Y. Zou ◽  
M. Jung ◽  
Th. Schmidt ◽  
R. Fink ◽  
...  

1991 ◽  
Vol 44 (2) ◽  
pp. 184-190 ◽  
Author(s):  
S Svensson ◽  
M Carlsson-Göthe ◽  
L Karlsson ◽  
A Nilsson ◽  
N Mårtensson ◽  
...  

1989 ◽  
Vol 53 (370) ◽  
pp. 239-244 ◽  
Author(s):  
J. Purton ◽  
D. S. Urch

AbstractHigh-resolution X-ray emission spectra (XES) are presented for minerals with a variety of structures. The participation of the Si 3p orbitals in bonding is influenced by the local structure around the silicon atom. In orthosilicates the distortion of the SiO44--tetrahedron influences both peak-width and the intensity of the high-energy shoulder of the Si-Kβ spectrum. In minerals containing Si-O-Si bonds there is mixing of the Si 3s and 3p orbitals giving rise to a peak on the low-energy side of the main Si-Kβ peak. When combined with X-ray photoelectron spectra (XPS), a complete molecular orbital picture of bonding can be established.


1992 ◽  
Vol 58 (3) ◽  
pp. 185-197 ◽  
Author(s):  
M.Y. Adam ◽  
M.P. Keane ◽  
A. Naves de Brito ◽  
N. Correia ◽  
P. Baltzer ◽  
...  

1992 ◽  
Vol 164 (1) ◽  
pp. 123-129 ◽  
Author(s):  
M.Y. Adam ◽  
M.P. Keane ◽  
A. Naves de Brito ◽  
N. Correia ◽  
B. Wannberg ◽  
...  

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.


Author(s):  
G. Van Tendeloo ◽  
J. Van Landuyt ◽  
S. Amelinckx

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.


Author(s):  
R. Gronsky

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.


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