Results 261 to 270 of about 6,328,527 (298)
Two datasets are better than one: method of double moments for 3D reconstruction in cryo-EM. [PDF]
Inverse ProblKileel J, Mickelin O, Singer A, Xu S.
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Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.
BloodStojanovski BM +3 more
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AlignPCA-2D: PCA-reduced Euclidean vector alignment for 2D classification in cryo-EM. [PDF]
Acta Crystallogr D Struct BiolRamírez-Aportela E +6 more
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Cryo-EM image processing of amyloid filaments in RELION-5.1
Lövestam S +4 more
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Chemical Reviews, 2022
While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study synthetic soft matter noncovalent polymers has been much more limited.
Fengbin Wang +4 more
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While the application of cryogenic electron microscopy (cryo-EM) to helical polymers in biology has a long history, due to the huge number of helical macromolecular assemblies in viruses, bacteria, archaea, and eukaryotes, the use of cryo-EM to study synthetic soft matter noncovalent polymers has been much more limited.
Fengbin Wang +4 more
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Current Opinion in Structural Biology, 2018
Ribosomes and electron cryomicroscopy (cryo-EM) share a long, intertwined history. However, cryo-EM only recently usurped X-ray crystallography as the predominant structural method to study ribosomes in atomic detail. The main, but not only, reason for this succession was the introduction of direct-electron detectors enabling cryo-EM to achieve equally
Alan, Brown, Sichen, Shao
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Ribosomes and electron cryomicroscopy (cryo-EM) share a long, intertwined history. However, cryo-EM only recently usurped X-ray crystallography as the predominant structural method to study ribosomes in atomic detail. The main, but not only, reason for this succession was the introduction of direct-electron detectors enabling cryo-EM to achieve equally
Alan, Brown, Sichen, Shao
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Physiology, 2006
Cryoelectronmicroscopy is a method for the imaging of macromolecules in the electron microscope. It was originally developed to determine membrane protein structures from two-dimensional crystals, but more recently “single-particle” techniques have become powerful and popular. Three-dimensional reconstructions are obtained from sets of single-particle
Liguo, Wang, Fred J, Sigworth
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Cryoelectronmicroscopy is a method for the imaging of macromolecules in the electron microscope. It was originally developed to determine membrane protein structures from two-dimensional crystals, but more recently “single-particle” techniques have become powerful and popular. Three-dimensional reconstructions are obtained from sets of single-particle
Liguo, Wang, Fred J, Sigworth
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Multiparticle Cryo-EM of Ribosomes
2010As the resolution of cryo-EM reconstructions has improved to the subnanometer range, conformational and compositional heterogeneity have become increasing problems in cryo-EM, limiting the resolution of reconstructions. Since further purification is not feasible, the presence of several conformational states of ribosomal complexes in thermodynamic ...
Justus, Loerke +2 more
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Science, 1999
Cryoelectron microscopy (cryo-EM) combined with three-dimensional image reconstruction techniques allows researchers to view macromolecular structures at resolutions below 10 A. Cryo-EM has thus become an alternative method for solving the structure of biomolecules that remain beyond the reach of nuclear magnetic resonance (NMR) or x-ray ...
R, Peters, R, Sikorski
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Cryoelectron microscopy (cryo-EM) combined with three-dimensional image reconstruction techniques allows researchers to view macromolecular structures at resolutions below 10 A. Cryo-EM has thus become an alternative method for solving the structure of biomolecules that remain beyond the reach of nuclear magnetic resonance (NMR) or x-ray ...
R, Peters, R, Sikorski
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Current Opinion in Structural Biology, 2018
ATP synthases are rotary enzymes found in bacteria, chloroplasts, and mitochondria. These complexes produce the majority of cellular ATP in aerobic cells using energy from the transmembrane proton motive force established by the electron transport chain.
Hui Guo, John L Rubinstein
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ATP synthases are rotary enzymes found in bacteria, chloroplasts, and mitochondria. These complexes produce the majority of cellular ATP in aerobic cells using energy from the transmembrane proton motive force established by the electron transport chain.
Hui Guo, John L Rubinstein
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