Results 171 to 180 of about 1,110,843 (197)

Cryoelectron microscopy with elemental sensitivity

Structure
In a recent issue of Nature Methods, Pfeil-Gardiner et al. (2024)1 combine electron energy-loss spectroscopy and single-particle cryoelectron microscopy to allow the spatially resolved imaging of the elemental composition of macromolecules.
Hannah, Ochner, Tanmay A M, Bharat
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Structure of bluetongue virus particles by cryoelectron microscopy

Journal of Structural Biology, 1992
The structure of the bluetongue virus (BTV) particle, determined by cryoelectron microscopy and image analysis, reveals a well-ordered outer shell which differs markedly from other known Reoviridae. The inner shell is known to have an icosahedral structure with 260 triangular spikes of VP7 trimers arranged on a T = 13,l lattice. The outer shell is seen
E A, Hewat, T F, Booth, P, Roy
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Cryoultramicrotomy: cryoelectron microscopy of vitreous sections.

Methods in molecular biology (Clifton, N.J.), 2007
Cryoultramicrotomy allows the sectioning of vitrified biological samples. These biological samples are preserved at the atomic level and represent the real structure at the moment of freezing. Cryoultramicrotomy produces ultra-thin cryosections that are investigated in a cryoelectron microscope.
Vanhecke D, Studer L, Studer D
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A cryoelectron microscopy study of the interaction of theEscherichia coliF1-ATPase with subunitbdimer [PDF]

FEBS Letters, 1994
A complex between the Escherichia coli F1-ATPase and a truncated form of the ECF0-b subunit was formed and examined by cryoelectron microscopy in amorphous ice. Image analysis of single particles in the hexagonal projection revealed that the polar domain
Stanley Dunn, Roderick A Capaldi, S Wilkens   +2 more
exaly   +2 more sources

DNA at the Entry-Exit of the Nucleosome Observed by Cryoelectron Microscopy

Journal of Structural Biology, 1995
Whereas the DNA path inside the nucleosome is well established, it is essentially unknown in the "entry-exit" region, a missing piece in our understanding of the chromatin fiber's folding. The three-dimensional structure of "linker" DNA was investigated here on single nucleosomes reconstituted without H1 on a 256-bp DNA fragment.
Furrer P, Bednar J, Dubochet J, Hamiche A, Prunell A   +4 more
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Cryoelectron microscopy: from molecules to systems

2008
Cryo electron microscopy is a generic term referring to different imaging modalities as applied to samples embedded in vitreous ice. Thereby it combines a close-to-life preservation of biological materials with the potential of high-resolution threedimensional imaging [1].
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Cryoelectron Microscopy of Microtubules

Journal of Structural Biology, 1993
R H, Wade, D, Chrétien
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Structural Studies of Ca2+-ATPase by Cryoelectron Microscopy

1994
The Ca2+-ATPase from sarcoplasmic reticulum (SR) is exceedingly well characterized in terms of kinetics, ligand binding and amino acid sequence. For example, particular events in the reaction cycle have been assigned to specific amino acid residues by sitedirected mutagenesis and characterization of ligand binding.
D. L. Stokes, N. M. Green, C. Toyoshima
openaire   +1 more source

Recent Advances in Cryoelectron Microscopy

Annals of the New York Academy of Sciences, 1986
E, Zeitler, F, Zemlin
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Cryoelectron microscopy of Na + ,K + -ATPase in the two E2P states with and without cardiotonic steroids

Proceedings of the National Academy of Sciences of the United States of America, 2022
Chikashi Toyoshima, Bente Vilsen, Flemming Cornelius   +2 more
exaly