scholarly journals Wavelet-based analysis and power law classification of C/NOFS high-resolution electron density data

Radio Science ◽  
2014 ◽  
Vol 49 (8) ◽  
pp. 680-688 ◽  
Author(s):  
C. L. Rino ◽  
C. S. Carrano ◽  
Patrick Roddy
Keyword(s):  
High Resolution ◽  
Electron Density ◽  
Power Law ◽  
Density Data ◽  
Resolution Electron

Topological Analysis of Proteins as Derived from Medium and High-resolution Electron Density: Applications to Electrostatic Properties

2007 ◽  
pp. 285-315 ◽  
Author(s):  
Laurence Leherte ◽  
Benoît Guillot ◽  
Daniel P. Vercauteren ◽  
Virginie Pichon-Pesme ◽  
Christian Jelsch ◽  
...  
Keyword(s):  
High Resolution ◽  
Electron Density ◽  
Topological Analysis ◽  
Electrostatic Properties ◽  
Resolution Electron

High resolution electron density distribution determination for GaAs and CdTe

2001 ◽  
Vol 229 (1-4) ◽  
pp. 130-136 ◽  
Author(s):  
Tsuyoshi Kajitani ◽  
Ramachandran Saravanan ◽  
Yasuhiro Ono ◽  
Kaoru Ohno ◽  
Minoru Isshiki
Keyword(s):  
High Resolution ◽  
Density Distribution ◽  
Electron Density ◽  
Electron Density Distribution ◽  
Resolution Electron

A new method for the construction of coarse-grained models of large biomolecules from low-resolution cryo-electron microscopy data

2019 ◽  
Vol 21 (19) ◽  
pp. 9720-9727 ◽  
Author(s):  
Yuwei Zhang ◽  
Kelin Xia ◽  
Zexing Cao ◽  
Frauke Gräter ◽  
Fei Xia
Keyword(s):  
Electron Microscopy ◽  
Electron Density ◽  
Rapid Development ◽  
Coarse Grained ◽  
Low Resolution ◽  
Density Data ◽  
Cryo Electron Microscopy ◽  
Electron Microscopy Data ◽  
Resolution Electron ◽  
Microscopy Data

The rapid development of cryo-electron microscopy (cryo-EM) has led to the generation of significant low-resolution electron density data of biomolecules.

Light Optical Diffraction Studies of Macromolecular Ultrastructure

1970 ◽  
Vol 28 ◽  
pp. 258-259
Author(s):  
Glen B. Haydon
Keyword(s):  
High Resolution ◽  
Diffraction Analysis ◽  
Diffraction Pattern ◽  
Electron Micrographs ◽  
Optical Diffraction ◽  
Electron Micrograph ◽  
Its Analysis ◽  
Resolution Electron ◽  
Diffraction Patterns

Analysis of light optical diffraction patterns produced by electron micrographs can easily lead to much nonsense. Such diffraction patterns are referred to as optical transforms and are compared with transforms produced by a variety of mathematical manipulations. In the use of light optical diffraction patterns to study periodicities in macromolecular ultrastructures, a number of potential pitfalls have been rediscovered. The limitations apply to the formation of the electron micrograph as well as its analysis.(1) The high resolution electron micrograph is itself a complex diffraction pattern resulting from the specimen, its stain, and its supporting substrate. Cowley and Moodie (Proc. Phys. Soc. B, LXX 497, 1957) demonstrated changing image patterns with changes in focus. Similar defocus images have been subjected to further light optical diffraction analysis.

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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