Results 11 to 20 of about 68,000 (256)

Cryo-electron microscopy of viruses [PDF]

open access: yesNature, 1984
Thin vitrified layers of unfixed, unstained and unsupported virus suspensions can be prepared for observation by cryo-electron microscopy in easily controlled conditions. The viral particles appear free from the kind of damage caused by dehydration, freezing or adsorption to a support that is encountered in preparing biological samples for conventional
Adrian, Marc   +3 more
openaire   +6 more sources

Structural basis for genome packaging, retention, and ejection in human cytomegalovirus

open access: yesNature Communications, 2021
Human cytomegalovirus (HCMV) is the prototypical member of the β-herpesvirinae subfamily and the leading viral cause of congenital infections that can lead to birth defects and it can also cause life-threatening disease in immunocompromised individuals ...
Zhihai Li   +3 more
doaj   +1 more source

Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers

open access: yesNature Communications, 2023
The T5 family of viruses are tailed bacteriophages characterized by a long non-contractile tail. The bacteriophage DT57C is closely related to the paradigmal T5 phage, though it recognizes a different receptor (BtuB) and features highly divergent lateral
Rafael Ayala   +9 more
doaj   +1 more source

Biological cryo‐electron microscopy in China [PDF]

open access: yesProtein Science, 2016
AbstractCryo‐electron microscopy (cryo‐EM) plays an increasingly more important role in structural biology. With the construction of an arm of the Chinese National Protein Science Facility at Tsinghua University, biological cryo‐EM has entered a phase of rapid development in China. This article briefly reviews the history of biological cryo‐EM in China,
Hong‐Wei Wang, Jianlin Lei, Yigong Shi
openaire   +2 more sources

Measuring the effects of ice thickness on resolution in single particle cryo-EM

open access: yesJournal of Structural Biology: X, 2023
Ice thickness is a critical parameter in single particle cryo-EM – too thin ice can break during imaging or exclude the sample of interest, while ice that is too thick contributes to more inelastic scattering that precludes obtaining high resolution ...
Kasahun Neselu   +5 more
doaj   +1 more source

Cryo‐electron microscopy of vitreous sections [PDF]

open access: yesThe EMBO Journal, 2004
Since the beginning of the 1980s, cryo-electron microscopy of a thin film of vitrified aqueous suspension has made it possible to observe biological particles in their native state, in the absence of the usual artefacts of dehydration and staining.
Al-Amoudi, Ashraf   +9 more
openaire   +6 more sources

Best practice: setting up and operating a mid-sized cryo-EM facility

open access: yesFrontiers in Molecular Biosciences, 2023
Ever since the resolution revolution in 2013, cryo-electron microscopy (cryo-EM) has become a powerful methodology in structural biology that is especially suited to study the structure of large flexible molecular complexes.
Xing Meng   +8 more
doaj   +1 more source

4D Cryo-Electron Microscopy of Proteins [PDF]

open access: yesJournal of the American Chemical Society, 2013
Cryo-electron microscopy is a form of transmission electron microscopy that has been used to determine the 3D structure of biological specimens in the hydrated state and with high resolution. We report the development of 4D cryo-electron microscopy by integrating the fourth dimension, time, into this powerful technique.
Fitzpatrick, AWP   +3 more
openaire   +4 more sources

MATHEMATICS FOR CRYO-ELECTRON MICROSCOPY [PDF]

open access: yesProceedings of the International Congress of Mathematicians (ICM 2018), 2019
Proceedings of the International Congress of Mathematicians ...
openaire   +2 more sources

Cryo-electron Microscopy of Membrane Proteins [PDF]

open access: yes, 2013
Electron crystallography is used to study membrane proteins in the form of planar, two-dimensional (2D) crystals, or other crystalline arrays such as tubular crystals. This method has been used to determine the atomic resolution structures of bacteriorhodopsin, tubulin, aquaporins, and several other membrane proteins.
Goldie, Kenneth N   +5 more
openaire   +4 more sources

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