Results 41 to 50 of about 22,940 (199)

Morphology of influenza B/Lee/40 determined by cryo-electron microscopy. [PDF]

open access: yesPLoS ONE, 2014
Cryo-electron microscopy projection image analysis and tomography is used to describe the overall architecture of influenza B/Lee/40. Algebraic reconstruction techniques with utilization of volume elements (blobs) are employed to reconstruct tomograms of
Garrett Katz   +9 more
doaj   +1 more source

Cryo-electron microscopy of extracellular vesicles from cerebrospinal fluid.

open access: yesPLoS ONE, 2020
Extracellular vesicles (EVs) are membrane-enclosed vesicles which play important role for cell communication and physiology. EVs are found in many human biological fluids, including blood, breast milk, urine, cerebrospinal fluid (CSF), ejaculate, saliva ...
Anton Emelyanov   +10 more
doaj   +1 more source

Learning to automate cryo-electron microscopy data collection with Ptolemy

open access: yesIUCrJ, 2023
Over the past decade, cryo-electron microscopy (cryoEM) has emerged as an important method for determining near-native, near-atomic resolution 3D structures of biological macromolecules.
Paul T. Kim   +3 more
doaj   +1 more source

Membrane shape as a reporter for applied forces [PDF]

open access: yes, 2008
Recent advances have enabled 3-dimensional reconstructions of biological structures in vivo, ranging in size and complexity from single proteins to multicellular structures. In particular, tomography and confocal microscopy have been exploited to capture
Antonny   +30 more
core   +2 more sources

Quaternary organization of a phytochrome dimer as revealed by cryoelectron microscopy. [PDF]

open access: yesProc Natl Acad Sci U S A, 2010
Phytochromes are a collection of dimeric photoreceptors that direct a diverse array of responses in plants and microorganisms through photoconversion between a red light-absorbing ground state Pr, and a far-red light-absorbing photoactivated state Pfr.
Li H, Zhang J, Vierstra RD, Li H.
europepmc   +4 more sources

Bacterial selenocysteine synthase structure revealed by single-particle cryoEM

open access: yesCurrent Research in Structural Biology
The 21st amino acid, selenocysteine (Sec), is synthesized on its dedicated transfer RNA (tRNASec). In bacteria, Sec is synthesized from Ser-tRNA[Ser]Sec by Selenocysteine Synthase (SelA), which is a pivotal enzyme in the biosynthesis of Sec.
Vitor Hugo Balasco Serrão   +3 more
doaj   +1 more source

The stack: a new bacterial structure analyzed in the Antarctic bacterium Pseudomonas deceptionensis M1(T) by transmission electron microscopy and tomography. [PDF]

open access: yesPLoS ONE, 2013
In recent years, improvements in transmission electron microscopy (TEM) techniques and the use of tomography have provided a more accurate view of the complexity of the ultrastructure of prokaryotic cells. Cryoimmobilization of specimens by rapid cooling
Lidia Delgado   +4 more
doaj   +1 more source

Purification and Cryo-electron Microscopy Analysis of Plant Mitochondrial Ribosomes

open access: yesBio-Protocol, 2021
Plants make up by far the largest part of biomass on Earth. They are the primary source of food and the basis of most drugs used for medicinal purposes. Similarly to all eukaryotes, plant cells also use mitochondria for energy production.
Florent Waltz   +2 more
doaj   +1 more source

Lensfree super-resolution holographic microscopy using wetting films on a chip. [PDF]

open access: yes, 2011
We investigate the use of wetting films to significantly improve the imaging performance of lensfree pixel super-resolution on-chip microscopy, achieving < 1 µm spatial resolution over a large imaging area of ~24 mm(2).
Bishara, Waheb   +2 more
core   +1 more source

Cryoelectron Microscopy and Image Analysis of the Cardiac Ryanodine Receptor [PDF]

open access: yesJournal of Biological Chemistry, 1998
The three-dimensional structure of the cardiac muscle ryanodine receptor (RyR2) is described and compared with its skeletal muscle isoform (RyR1). Previously, structural studies of RyR2 have not been as informative as those for RyR1 because optimal conditions for electron microscopy, which require low levels of phospholipid, are destabilizing for RyR2.
M R, Sharma   +5 more
openaire   +2 more sources

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