Structure of planar defects in (Sr0.9Ca0.3)1.1CuO2 infinite-layer superconductors by quantitative high-resolution electron microscopy

1995 ◽  
Vol 57 (1) ◽  
pp. 103-111 ◽  
Author(s):  
H. Zhang ◽  
L.D. Marks ◽  
Y.Y. Wang ◽  
H. Zhang ◽  
V.P. Dravid ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Planar Defects ◽  
Infinite Layer ◽  
Resolution Electron

Nano-probe x-ray analysis and high-resolution imaging on planar defects in high-pressure synthesized infinite-layer superconductor

1994 ◽  
Vol 52 ◽  
pp. 728-729
Author(s):  
Y. Y. Wang ◽  
H. Zhang ◽  
V. P. Dravid ◽  
H. Zhang ◽  
L. D. Marks ◽  
...  
Keyword(s):  
High Pressure ◽  
High Resolution ◽  
Atomic Structure ◽  
Emission Spectra ◽  
High Resolution Electron Microscopy ◽  
Planar Defects ◽  
X Ray ◽  
Infinite Layer ◽  
Resolution Electron ◽  
Resolution Imaging

Azuma et al. observed planar defects in a high pressure synthesized infinitelayer compound (i.e. ACuO2 (A=cation)), which exhibits superconductivity at ~110 K. It was proposed that the defects are cation deficient and that the superconductivity in this material is related to the planar defects. In this report, we present quantitative analysis of the planar defects utilizing nanometer probe xray microanalysis, high resolution electron microscopy, and image simulation to determine the chemical composition and atomic structure of the planar defects. We propose an atomic structure model for the planar defects.Infinite-layer samples with the nominal chemical formula, (Sr1-xCax)yCuO2 (x=0.3; y=0.9,1.0,1.1), were prepared using solid state synthesized low pressure forms of (Sr1-xCax)CuO2 with additions of CuO or (Sr1-xCax)2CuO3, followed by a high pressure treatment.Quantitative x-ray microanalysis, with a 1 nm probe, was performed using a cold field emission gun TEM (Hitachi HF-2000) equipped with an Oxford Pentafet thin-window x-ray detector. The probe was positioned on the planar defects, which has a 0.74 nm width, and x-ray emission spectra from the defects were compared with those obtained from vicinity regions.

Recent trends in high-resolution electron microscopy

1986 ◽  
Vol 44 ◽  
pp. 530-533
Author(s):  
David J. Smith
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Two Dimensional ◽  
Planar Defects ◽  
Medium Voltage ◽  
Resolution Electron ◽  
Routine Basis ◽  
Recent Trends ◽  
Electron Microscopes

The recent advent of high-resolution electron microscopes (HREMs) capable of resolving sub-2-Ångstrom detail on a routine basis has led to an enormous increase in the range of materials which can be usefully studied. Not only is it possible to resolve individual atomic columns in low index zones of most common metals but observations of semiconductors, for example, are no longer restricted to the traditional [110] zone, thereby making it feasible at last to obtain two-dimensional information about surfaces, interfaces and other planar defects. There is a worldwide upsurge of interest in the capabilities of these machines and the so-called medium-voltage (300-400kV) HREMs are selling rapidly despite their considerable expense. Our objective here is to provide a brief and selective overview of the latest applications and likely trends in HREM studies of materials - further details can be found elsewhere in these proceedings. No attempt is made to review instrumentation developments since they are being considered separately.

High Resolution Tem of Semiconductor Defects

1980 ◽  
Vol 38 ◽  
pp. 282-285
Author(s):  
J. C. H. Spence
Keyword(s):  
Electron Microscopy ◽  
Electronic Structure ◽  
High Resolution ◽  
Recent Work ◽  
High Resolution Electron Microscopy ◽  
Unique Contribution ◽  
Resolution Limit ◽  
Planar Defects ◽  
Semiconductor Defects ◽  
Resolution Electron

Computational techniques are now well developed for the determination of the electronic structure of semiconductor surfaces and their line and planar defects. These calculations depend sensitively on the atomic structure assumed for the defect, and so provide an outstanding challenge for high resolution electron microscopy, while it is unlikely that the details of the charge redistribution which controls the electronic structure of defects will be directly imaged for many years, the use of a-priori chemical knowledge may frequently greatly limit the number of likely defect structures. New high resolution imaging methods for the study of surface roughness, an area of almost total ignorance, are described elsewhere in this volume (1). It seems likely that the electronic structure of the line and planar defects will only be solved when all the information available from such techniques as EPR, SDP Hall effect measurements, CTS and EBIC are considered (see (2) for a review of recent work). The unique contribution of high resolution electron microscopy (HREM) is its non-statistical capability of analysing isolated, well characterised defects. The outstanding problems which semiconductor defects offer for HREM are (i) the difficulty of obtaining three dimensional defect structure information (ii) the need to extract information beyond the point resolution limit of current machines (but within their information resolution limit (3)) (iii) the need for chemical (atomic number) information. These three problems are briefly discussed below in the light of recent work.

Structural analysis of the surface-layer protein of spirillum serpens by high-resolution electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 738-739
Author(s):  
W. H. Wu ◽  
R. M. Glaeser
Keyword(s):  
Electron Microscopy ◽  
Surface Layer ◽  
Structural Analysis ◽  
High Resolution ◽  
Low Dose ◽  
High Resolution Electron Microscopy ◽  
Optical Diffraction ◽  
Surface Layer Protein ◽  
Morphological Unit ◽  
Resolution Electron

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.

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.

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