scholarly journals 3-Dimensional Structure of Human Cardiac Muscle Myosin Filaments by Electron Microscopy and Single Particle Analysis

2012 ◽  
Vol 102 (3) ◽  
pp. 149a-150a ◽  
Author(s):  
Hind A. AL-Khayat ◽  
Robert W. Kensler ◽  
John M. Squire ◽  
Steve B. Marston ◽  
Edward P. Morris
Keyword(s):  
Electron Microscopy ◽  
Cardiac Muscle ◽  
Single Particle ◽  
Dimensional Structure ◽  
Particle Analysis ◽  
Single Particle Analysis ◽  
3 Dimensional ◽  
Myosin Filaments ◽  
Muscle Myosin

3D structure of relaxed fish muscle myosin filaments by single particle analysis

2006 ◽  
Vol 155 (2) ◽  
pp. 202-217 ◽  
Author(s):  
Hind A. AL-Khayat ◽  
Edward P. Morris ◽  
Robert W. Kensler ◽  
John M. Squire
Keyword(s):  
Single Particle ◽  
3D Structure ◽  
Fish Muscle ◽  
Particle Analysis ◽  
Single Particle Analysis ◽  
Myosin Filaments ◽  
Muscle Myosin

scholarly journals Electron microscopy snapshots of single particles from single cells

2018 ◽  
Vol 294 (5) ◽  
pp. 1602-1608 ◽  
Author(s):  
Xiunan Yi ◽  
Eric J. Verbeke ◽  
Yiran Chang ◽  
Daniel J. Dickinson ◽  
David W. Taylor
Keyword(s):  
Electron Microscopy ◽  
Single Particle ◽  
Protein Complexes ◽  
Signal To Noise Ratio ◽  
Single Cells ◽  
Particle Analysis ◽  
Biological Macromolecules ◽  
Single Particle Analysis ◽  
Whole Cells ◽  
Potential Applications

Cryo-electron microscopy (cryo-EM) has become an indispensable tool for structural studies of biological macromolecules. Two additional predominant methods are available for studying the architectures of multiprotein complexes: 1) single-particle analysis of purified samples and 2) tomography of whole cells or cell sections. The former can produce high-resolution structures but is limited to highly purified samples, whereas the latter can capture proteins in their native state but has a low signal-to-noise ratio and yields lower-resolution structures. Here, we present a simple, adaptable method combining microfluidic single-cell extraction with single-particle analysis by EM to characterize protein complexes from individual Caenorhabditis elegans embryos. Using this approach, we uncover 3D structures of ribosomes directly from single embryo extracts. Moreover, we investigated structural dynamics during development by counting the number of ribosomes per polysome in early and late embryos. This approach has significant potential applications for counting protein complexes and studying protein architectures from single cells in developmental, evolutionary, and disease contexts.

scholarly journals Single particle analysis of clamp loader by electron microscopy

1999 ◽  
Vol 39 (supplement) ◽  
pp. S111
Author(s):  
K. Mayanagi ◽  
T. Miyata ◽  
K. Morikawa ◽  
I. Cann ◽  
S. Ishino ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Single Particle ◽  
Particle Analysis ◽  
Single Particle Analysis ◽  
Clamp Loader

scholarly journals The Resolution in X-ray Crystallography and Single-Particle Cryogenic Electron Microscopy

Crystals ◽  
2020 ◽  
Vol 10 (7) ◽  
pp. 580
Author(s):  
Victor R.A. Dubach ◽  
Albert Guskov
Keyword(s):  
Electron Microscopy ◽  
Single Particle ◽  
Signal To Noise Ratio ◽  
Three Dimensional ◽  
Particle Analysis ◽  
Biological Macromolecules ◽  
Single Particle Analysis ◽  
X Ray ◽  
X Ray Crystallography ◽  
The Fourier Transform

X-ray crystallography and single-particle analysis cryogenic electron microscopy are essential techniques for uncovering the three-dimensional structures of biological macromolecules. Both techniques rely on the Fourier transform to calculate experimental maps. However, one of the crucial parameters, resolution, is rather broadly defined. Here, the methods to determine the resolution in X-ray crystallography and single-particle analysis are summarized. In X-ray crystallography, it is becoming increasingly more common to include reflections discarded previously by traditionally used standards, allowing for the inclusion of incomplete and anisotropic reflections into the refinement process. In general, the resolution is the smallest lattice spacing given by Bragg’s law for a particular set of X-ray diffraction intensities; however, typically the resolution is truncated by the user during the data processing based on certain parameters and later it is used during refinement. However, at which resolution to perform such a truncation is not always clear and this makes it very confusing for the novices entering the structural biology field. Furthermore, it is argued that the effective resolution should be also reported as it is a more descriptive measure accounting for anisotropy and incompleteness of the data. In single particle cryo-EM, the situation is not much better, as multiple ways exist to determine the resolution, such as Fourier shell correlation, spectral signal-to-noise ratio and the Fourier neighbor correlation. The most widely accepted is the Fourier shell correlation using a threshold of 0.143 to define the resolution (so-called “gold-standard”), although it is still debated whether this is the correct threshold. Besides, the resolution obtained from the Fourier shell correlation is an estimate of varying resolution across the density map. In reality, the interpretability of the map is more important than the numerical value of the resolution.

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