High‐resolution electron microscopy analysis of Nd‐Fe‐B‐type sintered magnets

1991 ◽  
Vol 69 (8) ◽  
pp. 5510-5511 ◽  
Author(s):  
Jinfang Liu ◽  
Helie Luo ◽  
Shuming Pan ◽  
Yuan Sun ◽  
Guoshun Shi
2005 ◽  
Vol 85 (2) ◽  
pp. 51-59 ◽  
Author(s):  
H. A. Calderon * ◽  
G. Kostorz ◽  
L. Calzado-Lopez ◽  
C. Kisielowski ◽  
T. Mori

2013 ◽  
Vol 19 (S2) ◽  
pp. 224-225
Author(s):  
J.A. Gaddy ◽  
T.L. Cover

Extended abstract of a paper presented at Microscopy and Microanalysis 2013 in Indianapolis, Indiana, USA, August 4 – August 8, 2013.


1994 ◽  
Vol 357 ◽  
Author(s):  
B. V. Vuchic ◽  
K. L. Merkle ◽  
D. B. Buchholz ◽  
R. P. H. Chang ◽  
L. D. Marks

AbstractIndividual 45° [001] tilt grain boundaries in Y1Ba2Cu3O7-x thin films grown on biepitaxial substrates were studied. The thin films were grown using both pulsed organometallic beam epitaxy (POMBE) and laser ablation. Transport characteristics of the individual grain boundaries were measured including resistance - temperature (R-T) and current - voltage (I-V) dependencies with and without an applied magnetic field. In order to elucidate possible structural origins of the differences in transport behavior, the same grain boundaries which were electrically characterized were subsequently thinned for electron-microscopy analysis. Transmission-electron-microscopy and high-resolution-electron-microscopy were used to structurally characterize the grain boundaries. The macroscopic and microscopic structures of two boundaries, a nominally resistive and a superconducting grain boundary, are compared.


Author(s):  
W. H. Wu ◽  
R. M. Glaeser

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.


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