scholarly journals High Resolution Structural Analysis Of ALS‐Associated Mutant SOD1 Inclusion Bodies

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Dalia Naser ◽  
Michael Tarasca ◽  
Gyana Mishra ◽  
Tyler Soule ◽  
Harmeen Deol ◽  
...  
Keyword(s):  
Structural Analysis ◽  
High Resolution ◽  
Inclusion Bodies ◽  
Mutant Sod1

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.

Europium-Doped Ceria–Gadolinium Mixed Oxides: PARAFAC Analysis and High-Resolution Emission Spectroscopy under Cryogenic Conditions for Structural Analysis

2020 ◽  
Vol 124 (24) ◽  
pp. 4972-4983
Author(s):  
Sitshengisiwe Chemura ◽  
Toni Haubitz ◽  
Philipp A. Primus ◽  
Martin Underberg ◽  
Tim Hülser ◽  
...  
Keyword(s):  
Structural Analysis ◽  
High Resolution ◽  
Emission Spectroscopy ◽  
Mixed Oxides ◽  
Doped Ceria ◽  
Cryogenic Conditions

X-ray computed microtomography for the structural analysis of jewelry from the Museum “Royal Tombs of Sipán”

2020 ◽  
Vol 35 (S1) ◽  
pp. S38-S42
Author(s):  
Soraia Rodrigues de Azeredo ◽  
Roberto Cesareo ◽  
Angel Guillermo Bustamante Dominguez ◽  
Ricardo Tadeu Lopes
Keyword(s):  
Structural Analysis ◽  
High Resolution ◽  
Copper Alloys ◽  
North Coast ◽  
Flat Panel ◽  
X Ray ◽  
The North ◽  
Gold Silver ◽  
Computed Microtomography ◽  
X Ray Computed

Precious ornaments from the Museum Royal Tombs of Sipán were analyzed by X-ray computed microtomography (microCT). The ornaments analyzed were golden earrings produced by the Moche culture that flourished along the north coast of present-day Peru between approximately 100 and 600 AD. Sipán, also known as Huava Rajada, is a mochica archaeological complex in the north of Peru. In particular, the spectacular jewelry, mainly composed of gold, silver, and copper alloys, gilded copper, and tumbaga, from the Museum “Royal Tombs of Sipán,” in Lambayeque, north of Peru, are some of the most sophisticated metalworking ever produced of pre-Columbian America. A portable microCT system consisting of a high-resolution flat panel detector and a mini X-ray tube were used for the structural analysis of these ornaments. The microCT images show parts of the internal structure, highlighting the manufacturing technique and gold sheets joining techniques of the Moche artisans. Furthermore, the advantage of using the portable microCT system for nondestructive testing is clear when the sample cannot be taken to the laboratory.

scholarly journals High-resolution dislocation imaging and micro-structural analysis of HVPE-βGa2O3 films using monochromatic synchrotron topography

APL Materials ◽  
2019 ◽  
Vol 7 (2) ◽  
pp. 022513 ◽  
Author(s):  
Nadeemullah A. Mahadik ◽  
Marko J. Tadjer ◽  
Peter L. Bonanno ◽  
Karl D. Hobart ◽  
Robert E. Stahlbush ◽  
...  
Keyword(s):  
Structural Analysis ◽  
High Resolution ◽  
Monochromatic Synchrotron

Structural analysis of Aleksinac oil shale kerogen by high-resolution solid-state 13C n.m.r. spectroscopy

Fuel ◽  
1995 ◽  
Vol 74 (12) ◽  
pp. 1903-1909 ◽  
Author(s):  
Zoran Ẑujović ◽  
Radivoje Srejić ◽  
Dušan Vučelić ◽  
Dragomir Vitorović ◽  
Branimir Jovančićević
Keyword(s):  
Solid State ◽  
Structural Analysis ◽  
High Resolution ◽  
Oil Shale

scholarly journals High-Resolution Single-Molecule FRET via DNA eXchange (FRET X)

2020 ◽  
Author(s):  
Mike Filius ◽  
Sung Hyun Kim ◽  
Ivo Severins ◽  
Chirlmin Joo
Keyword(s):  
Structural Analysis ◽  
High Resolution ◽  
Single Molecule ◽  
Single Object ◽  
Single Molecule Fret ◽  
Dna Strands ◽  
Versatile Tool ◽  
Fret Efficiency ◽  
Fret Pair

ABSTRACTSingle-molecule FRET is a versatile tool to study nucleic acids and proteins at the nanometer scale. However, currently, only a couple of FRET pairs can be reliably measured on a single object. The limited number of available FRET pair fluorophores and complicated data analysis makes it challenging to apply single-molecule FRET for structural analysis of biomolecules. Currently, only a couple of FRET pairs can be reliably measured on a single object. Here we present an approach that allows for the determination of multiple distances between FRET pairs in a single object. We use programmable, transient binding between short DNA strands to resolve the FRET efficiency of multiple fluorophore pairs. By allowing only a single FRET pair to be formed at a time, we can determine the FRET efficiency and pair distance with sub-nanometer resolution. We determine the distance between other pairs by sequentially exchanging DNA strands. We name this multiplexing approach FRET X for FRET via DNA eXchange. We envision that our FRET X technology will be a tool for the high-resolution structural analysis of biomolecules and other nano-structures.

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