Three-dimensional reconstruction of bovine brain V-ATPase by cryo-electron microscopy and single particle analysis

2007 ◽  
Vol 158 (3) ◽  
pp. 445-454 ◽  
Author(s):  
Marco Gregorini ◽  
Jin Wang ◽  
Xiao-Song Xie ◽  
Ronald A. Milligan ◽  
Andreas Engel
Keyword(s):  
Electron Microscopy ◽  
Single Particle ◽  
Three Dimensional ◽  
Bovine Brain ◽  
Particle Analysis ◽  
Single Particle Analysis ◽  
Three Dimensional Reconstruction ◽  
Cryo Electron Microscopy ◽  
Dimensional Reconstruction

scholarly journals Three Dimensional Reconstruction of CFTR Chloride Channel Using Single Particle Analysis

2009 ◽  
Vol 96 (3) ◽  
pp. 468a
Author(s):  
Kazuhiro Mio ◽  
Toshihiko Ogura ◽  
Muneyo Mio ◽  
Hiroyasu Shimizu ◽  
Tzyh-Chang Hwang ◽  
...  
Keyword(s):  
Single Particle ◽  
Chloride Channel ◽  
Three Dimensional ◽  
Particle Analysis ◽  
Single Particle Analysis ◽  
Three Dimensional Reconstruction ◽  
Dimensional Reconstruction

Three-dimensional reconstruction of the muscle thin filament. Single particle analysis of an asymmetric filament

2008 ◽  
Vol 14 (S2) ◽  
pp. 1296-1297
Author(s):  
DM Paul ◽  
EP Morris ◽  
RW Kensler ◽  
JM Squire
Keyword(s):  
New Mexico ◽  
Single Particle ◽  
Thin Filament ◽  
Three Dimensional ◽  
Particle Analysis ◽  
Single Particle Analysis ◽  
Three Dimensional Reconstruction ◽  
Dimensional Reconstruction ◽  
Muscle Thin Filament

Extended abstract of a paper presented at Microscopy and Microanalysis 2008 in Albuquerque, New Mexico, USA, August 3 – August 7, 2008

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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