Full three-dimensional characterization of 25 nm lines for chemically amplified resist simulation

Author(s):  
S. Landis ◽  
S. Pauliac ◽  
J. Foucher ◽  
J. Thiault ◽  
F. de Crecy
2010 ◽  
Author(s):  
Jedsada Manyam ◽  
Mayandithevar Manickam ◽  
Jon A. Preece ◽  
Richard E. Palmer ◽  
Alex P. Robinson

2001 ◽  
Author(s):  
Benjamen M. Rathsack ◽  
Cyrus E. Tabery ◽  
Jeff A. Albelo ◽  
Peter D. Buck ◽  
C. Grant Willson

Author(s):  
Toshiro Itani ◽  
Minoru Toriumi ◽  
Takuya Naito ◽  
Seiichi Ishikawa ◽  
Seiro Miyoshi ◽  
...  

1997 ◽  
Vol 10 (4) ◽  
pp. 609-612 ◽  
Author(s):  
Teruhiko Kumada ◽  
Hiroshi Adachi ◽  
Hiroshi Watanabe ◽  
Hiroaki Sumitani

1999 ◽  
Author(s):  
Benjamen M. Rathsack ◽  
Cyrus E. Tabery ◽  
Timothy B. Stachowiak ◽  
Tim E. Dallas ◽  
Cheng-Bai Xu ◽  
...  

1999 ◽  
Vol 38 (Part 1, No. 12B) ◽  
pp. 7094-7098 ◽  
Author(s):  
Eun-Mi Lee ◽  
Moon-Gyu Sung ◽  
Young-Mi Lee ◽  
Young-Soo Sohn ◽  
Hye-Keun Oh

Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.


Author(s):  
J. A. Eades ◽  
A. E. Smith ◽  
D. F. Lynch

It is quite simple (in the transmission electron microscope) to obtain convergent-beam patterns from the surface of a bulk crystal. The beam is focussed onto the surface at near grazing incidence (figure 1) and if the surface is flat the appropriate pattern is obtained in the diffraction plane (figure 2). Such patterns are potentially valuable for the characterization of surfaces just as normal convergent-beam patterns are valuable for the characterization of crystals.There are, however, several important ways in which reflection diffraction from surfaces differs from the more familiar electron diffraction in transmission.GeometryIn reflection diffraction, because of the surface, it is not possible to describe the specimen as periodic in three dimensions, nor is it possible to associate diffraction with a conventional three-dimensional reciprocal lattice.


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