scholarly journals Three-Dimensional Structure of the M-region (Bare Zone) of Vertebrate Striated Muscle Myosin Filaments by Single-Particle Analysis

2010 ◽  
Vol 403 (5) ◽  
pp. 763-776 ◽  
Author(s):  
Hind A. AL-Khayat ◽  
Robert W. Kensler ◽  
Edward P. Morris ◽  
John M. Squire
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

2006 ◽  
Vol 155 (2) ◽  
pp. 202-217 ◽  
Author(s):  
Hind A. AL-Khayat ◽  
Edward P. Morris ◽  
Robert W. Kensler ◽  
John M. Squire

2009 ◽  
Vol 96 (3) ◽  
pp. 468a
Author(s):  
Kazuhiro Mio ◽  
Toshihiko Ogura ◽  
Muneyo Mio ◽  
Hiroyasu Shimizu ◽  
Tzyh-Chang Hwang ◽  
...  

Soft Matter ◽  
2018 ◽  
Vol 14 (48) ◽  
pp. 9750-9754 ◽  
Author(s):  
Daniel Zalami ◽  
Oliver Grimm ◽  
Felix H. Schacher ◽  
Uwe Gerken ◽  
Jürgen Köhler

Single-particle orbit tracking for characterising the 3d morphology of liquid-filled nanoporous structures.


Crystals ◽  
2020 ◽  
Vol 10 (7) ◽  
pp. 580
Author(s):  
Victor R.A. Dubach ◽  
Albert Guskov

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.


Sign in / Sign up

Export Citation Format

Share Document