scholarly journals Morphology of gold nanoparticles determined by full-curve fitting of the light absorption spectrum. Comparison with X-ray scattering and electron microscopy data

Nanoscale ◽  
2014 ◽  
Vol 6 (22) ◽  
pp. 13527-13534 ◽  
Author(s):  
Kostyantyn Slyusarenko ◽  
Benjamin Abécassis ◽  
Patrick Davidson ◽  
Doru Constantin
Keyword(s):  
Electron Microscopy ◽  
Gold Nanoparticles ◽  
Absorption Spectrum ◽  
Curve Fitting ◽  
Light Absorption ◽  
Full Curve ◽  
X Ray ◽  
X Ray Scattering ◽  
Electron Microscopy Data ◽  
Microscopy Data

scholarly journals Comparative characterisation of non-monodisperse gold nanoparticle populations by X-ray scattering and electron microscopy

Nanoscale ◽  
2020 ◽  
Vol 12 (22) ◽  
pp. 12007-12013
Author(s):  
Ye Yang ◽  
Suiyang Liao ◽  
Zhi Luo ◽  
Runzhang Qi ◽  
Niamh Mac Fhionnlaoich ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Gold Nanoparticles ◽  
Monte Carlo ◽  
Image Analysis ◽  
Small Angle ◽  
Method Comparison ◽  
X Ray ◽  
X Ray Scattering ◽  
Transmission Electron ◽  
Ray Scattering

A cross-method comparison for quasi-monodisperse, polydisperse and bimodal gold nanoparticles of 2–7 nm in diameter between conventional image analysis of transmission electron micrographs and small-angle X-ray scattering with form-free Monte Carlo fitting.

scholarly journals New wwPDB validation pipelines for X-ray, NMR and 3DEM structures

2014 ◽  
Vol 70 (a1) ◽  
pp. C1478-C1478
Author(s):  
Swanand Gore ◽  
Pieter Hendrickx ◽  
Eduardo Sanz-Garcia ◽  
Sameer Velankar ◽  
Gerard Kleywegt
Keyword(s):  
Electron Microscopy ◽  
Protein Data Bank ◽  
Data Bank ◽  
X Ray ◽  
Task Forces ◽  
Annotation System ◽  
Electron Microscopy Data ◽  
Microscopy Data ◽  
Machine Readable

The Protein Data Bank (PDB) is the single global archive of 3D biomacromolecular structure data. The archive is managed by the Worldwide Protein Data Bank (wwPDB; wwpdb.org) organisation through its partners, the Research Collaboratory for Structural Bioinformatics (RCSB PDB), the Protein Data Bank Japan (PDBj), the Protein Data Bank in Europe and the Biological Magnetic Resonance Bank (BMRB). Analogously, the Electron Microscopy Data Bank (EMDB) is managed by the EMDataBank (emdatabank.org) organisation. A few years ago, realising the needs and opportunities to assess the quality of biomacromolecular structures deposited in the PDB, the wwPDB and EMDataBank partners established Validation Task Forces (VTFs) to advice them on up-to-date and community-agreed methods and standards to validate X-ray, NMR and 3DEM structures and data. All three VTFs have now published their recommendations (1, 2, 3) and these are getting implemented as validation-software pipelines . The pipelines are integrated in the new joint wwPDB deposition and annotation system (http://deposit.wwpdb.org/deposition/). In addition, stand-alone servers are provided to allow practising structural biologists to validate models prior to publication and deposition (http://wwpdb.org/validation-servers.html). The validation pipelines and the output they produce (human-readable PDF reports and machine-readable XML files) will be described.

scholarly journals X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42

Data in Brief ◽  
2016 ◽  
Vol 8 ◽  
pp. 108-113 ◽  
Author(s):  
Olga M. Selivanova ◽  
Elizaveta I. Grigorashvili ◽  
Mariya Yu. Suvorina ◽  
Ulyana F. Dzhus ◽  
Alexey D. Nikulin ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Amyloid Formation ◽  
X Ray Diffraction ◽  
X Ray ◽  
Electron Microscopy Data ◽  
Microscopy Data

Microtubule nucleation sequence studied by time-resolved x-ray scattering and electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 766-767
Author(s):  
Eva-Maria Mandelkow ◽  
Eckhard Mandelkow ◽  
Joan Bordas
Keyword(s):  
Electron Microscopy ◽  
Dynamic Equilibrium ◽  
Time Resolved ◽  
X Ray ◽  
Additional Information ◽  
X Ray Scattering ◽  
Low Concentrations ◽  
Microtubule Growth ◽  
Ray Patterns ◽  
Ray Scattering

When a solution of microtubule protein is changed from non-polymerising to polymerising conditions (e.g. by temperature jump or mixing with GTP) there is a series of structural transitions preceding microtubule growth. These have been detected by time-resolved X-ray scattering using synchrotron radiation, and they may be classified into pre-nucleation and nucleation events. X-ray patterns are good indicators for the average behavior of the particles in solution, but they are difficult to interpret unless additional information on their structure is available. We therefore studied the assembly process by electron microscopy under conditions approaching those of the X-ray experiment. There are two difficulties in the EM approach: One is that the particles important for assembly are usually small and not very regular and therefore tend to be overlooked. Secondly EM specimens require low concentrations which favor disassembly of the particles one wants to observe since there is a dynamic equilibrium between polymers and subunits.

Time-Resolved Cryo-Electron Microscopy of Oscillating Microtubules

1990 ◽  
Vol 48 (1) ◽  
pp. 502-503
Author(s):  
Eva-Maria Mandelkow ◽  
Ron Milligan
Keyword(s):  
Electron Microscopy ◽  
Dynamic Instability ◽  
Entire Solution ◽  
Reaction Scheme ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
A Chain ◽  
Ray Scattering

Microtubules form part of the cytoskeleton of eukaryotic cells. They are hollow libers of about 25 nm diameter made up of 13 protofilaments, each of which consists of a chain of heterodimers of α-and β-tubulin. Microtubules can be assembled in vitro at 37°C in the presence of GTP which is hydrolyzed during the reaction, and they are disassembled at 4°C. In contrast to most other polymers microtubules show the behavior of “dynamic instability”, i.e. they can switch between phases of growth and phases of shrinkage, even at an overall steady state [1]. In certain conditions an entire solution can be synchronized, leading to autonomous oscillations in the degree of assembly which can be observed by X-ray scattering (Fig. 1), light scattering, or electron microscopy [2-5]. In addition such solutions are capable of generating spontaneous spatial patterns [6].In an earlier study we have analyzed the structure of microtubules and their cold-induced disassembly by cryo-EM [7]. One result was that disassembly takes place by loss of protofilament fragments (tubulin oligomers) which fray apart at the microtubule ends. We also looked at microtubule oscillations by time-resolved X-ray scattering and proposed a reaction scheme [4] which involves a cyclic interconversion of tubulin, microtubules, and oligomers (Fig. 2). The present study was undertaken to answer two questions: (a) What is the nature of the oscillations as seen by time-resolved cryo-EM? (b) Do microtubules disassemble by fraying protofilament fragments during oscillations at 37°C?

scholarly journals Alpha helical surfactant-like peptides self-assemble into pH-dependent nanostructures

Soft Matter ◽  
2021 ◽  
Vol 17 (11) ◽  
pp. 3096-3104
Author(s):  
Valeria Castelletto ◽  
Jani Seitsonen ◽  
Janne Ruokolainen ◽  
Ian W. Hamley
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Small Angle ◽  
Self Assembly ◽  
X Ray ◽  
Cryogenic Transmission Electron Microscopy ◽  
X Ray Scattering ◽  
Transmission Electron ◽  
Ph Dependent ◽  
Ray Scattering

A designed surfactant-like peptide is shown, using a combination of cryogenic-transmission electron microscopy and small-angle X-ray scattering, to have remarkable pH-dependent self-assembly properties.

scholarly journals Label-free fluorescence predictions from large-scale correlative light and electron microscopy data

2021 ◽  
Vol 27 (S1) ◽  
pp. 94-95
Author(s):  
Ryan Lane ◽  
Luuk Balkenende ◽  
Simon van Staalduine ◽  
Anouk Wolters ◽  
Ben Giepmans ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Large Scale ◽  
Light And Electron Microscopy ◽  
Label Free ◽  
Electron Microscopy Data ◽  
Microscopy Data
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