Structure of Amyloid Fibrils after Negative Staining and High-resolution Electron Microscopy

Nature ◽  
1965 ◽  
Vol 206 (4985) ◽  
pp. 737-738 ◽  
Author(s):  
TSURANOBU SHIRAHAMA ◽  
ALAN S. COHEN
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Amyloid Fibrils ◽  
High Resolution Electron Microscopy ◽  
Negative Staining ◽  
Resolution Electron

scholarly journals HIGH-RESOLUTION ELECTRON MICROSCOPIC ANALYSIS OF THE AMYLOID FIBRIL

1967 ◽  
Vol 33 (3) ◽  
pp. 679-708 ◽  
Author(s):  
Tsuranobu Shirahama ◽  
Alan S. Cohen
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Microscopic Analysis ◽  
High Resolution Electron Microscopy ◽  
Ultrastructural Organization ◽  
Electron Microscopic ◽  
Tissue Sections ◽  
Resolution Electron

The ultrastructural organization of the fibrous component of amyloid has been analyzed by means of high resolution electron microscopy of negatively stained isolated amyloid fibrils and of positively stained amyloid fibrils in thin tissue sections. It was found that a number of subunits could be resolved according to their dimensions. The following structural organization is proposed. The amyloid fibril, the fibrous component of amyloid as seen in electron microscopy of thin tissue sections, consists of a number of filaments aggregated side-by-side. These amyloid filaments are approximately 75–80 A in diameter and consist of five (or less likely six) subunits (amyloid protofibrils) which are arranged parallel to each other, longitudinal or slightly oblique to the long axis of the filament. The filament has often seemed to disperse into several longitudinal rows. The amyloid protofibril is about 25–35 A wide and appears to consist of two or three subunit strands helically arranged with a 35–50-A repeat (or, less likely, is composed of globular subunits aggregated end-to-end). These amyloid subprotofibrillar strands measure approximately 10–15 A in diameter.

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.

High resolution electron microscopy of lanthanum phosphate crystals

1978 ◽  
Vol 36 (1) ◽  
pp. 274-275
Author(s):  
J. C. Wheatley ◽  
J. M. Cowley
Keyword(s):  
Electron Microscopy ◽  
Catalytic Activity ◽  
High Resolution ◽  
Petroleum Industry ◽  
High Resolution Electron Microscopy ◽  
Lanthanum Phosphate ◽  
Good Catalyst ◽  
Resolution Electron ◽  
Good Catalytic Activity ◽  
Physical And Chemical

Rare-earth phosphates are of particular interest because of their catalytic properties associated with the hydrolysis of many aromatic chlorides in the petroleum industry. Lanthanum phosphates (LaPO4) which have been doped with small amounts of copper have shown increased catalytic activity (1). However the physical and chemical characteristics of the samples leading to good catalytic activity are not known.Many catalysts are amorphous and thus do not easily lend themselves to methods of investigation which would include electron microscopy. However, the LaPO4, crystals are quite suitable samples for high resolution techniques.The samples used were obtained from William L. Kehl of Gulf Research and Development Company. The electron microscopy was carried out on a JEOL JEM-100B which had been modified for high resolution microscopy (2). Standard high resolution techniques were employed. Three different sample types were observed: 669A-1-5-7 (poor catalyst), H-L-2 (good catalyst) and 27-011 (good catalyst).

Possible applications of fraunhofer holography in high resolution electron microscopy

1978 ◽  
Vol 36 (1) ◽  
pp. 222-223 ◽  
Author(s):  
N. Bonnet ◽  
M. Troyon ◽  
P. Gallion
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Transfer Function ◽  
Radiation Damage ◽  
High Resolution Electron Microscopy ◽  
Far Field ◽  
Field Region ◽  
Crystalline Materials ◽  
Resolution Electron ◽  
The Ideal

Two main problems in high resolution electron microscopy are first, the existence of gaps in the transfer function, and then the difficulty to find complex amplitude of the diffracted wawe from registered intensity. The solution of this second problem is in most cases only intended by the realization of several micrographs in different conditions (defocusing distance, illuminating angle, complementary objective apertures…) which can lead to severe problems of contamination or radiation damage for certain specimens.Fraunhofer holography can in principle solve both problems stated above (1,2). The microscope objective is strongly defocused (far-field region) so that the two diffracted beams do not interfere. The ideal transfer function after reconstruction is then unity and the twin image do not overlap on the reconstructed one.We show some applications of the method and results of preliminary tests.Possible application to the study of cavitiesSmall voids (or gas-filled bubbles) created by irradiation in crystalline materials can be observed near the Scherzer focus, but it is then difficult to extract other informations than the approximated size.

The observation of solutions in Ni3Nb

1988 ◽  
Vol 46 ◽  
pp. 540-541
Author(s):  
Z.M. Wang ◽  
J.P. Zhang
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Phase Modulation ◽  
High Resolution Electron Microscopy ◽  
Antiphase Domain ◽  
Boundary Area ◽  
Matrix Type ◽  
Resolution Electron ◽  
Domain Boundaries ◽  
Kontorova Model

High resolution electron microscopy reveals that antiphase domain boundaries in β-Ni3Nb have a hexagonal unit cell with lattice parameters ah=aβ and ch=bβ, where aβ and bβ are of the orthogonal β matrix. (See Figure 1.) Some of these boundaries can creep “upstairs” leaving an incoherent area, as shown in region P. When the stepped boundaries meet each other, they do not lose their own character. Our consideration in this work is to estimate the influnce of the natural misfit δ{(ab-aβ)/aβ≠0}. Defining the displacement field at the boundary as a phase modulation Φ(x), following the Frenkel-Kontorova model [2], we consider the boundary area to be made up of a two unit chain, the upper portion of which can move and the lower portion of the β matrix type, assumed to be fixed. (See the schematic pattern in Figure 2(a)).

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