Results 11 to 20 of about 1,110,843 (197)
Residue-level error detection in cryoelectron microscopy models. [PDF]
Building accurate protein models into moderate resolution (3-5 Å) cryoelectron microscopy (cryo-EM) maps is challenging and error prone. We have developed MEDIC (Model Error Detection in Cryo-EM), a robust statistical model that identifies local backbone errors in protein structures built into cryo-EM maps by combining local fit-to-density with deep ...
Reggiano G +4 more
europepmc +5 more sources
Cryoelectron Microscopy of Vitrified Specimens [PDF]
Water is the most abundant component of biological material, but it is systematically excluded from conventional electron microscopy. This is because water evaporates rapidly under the vacuum conditions of an electron microscope. Cryoelectron microscopy has long been seen as a possible avenue to overcome this limitation, but until recently the direct ...
Dubochet, Jacques +4 more
openaire +4 more sources
Cryoelectron Microscopy of Mouse Mammary Tumor Virus [PDF]
ABSTRACT Cryoelectron microscopy of Mouse mammary tumor virus , a Betaretrovirus , provided information about glycoprotein structure and core formation. The virions showed the broad range of diameters typical of retroviruses.
Briggs, J. +3 more
openaire +4 more sources
Cryoelectron Microscopy Structure of Purified γ-Secretase at 12 Å Resolution [PDF]
Gamma-secretase, an integral membrane protein complex, catalyzes the intramembrane cleavage of the beta-amyloid precursor protein (APP) during the neuronal production of the amyloid beta-peptide. As such, the protease has emerged as a key target for developing agents to treat and prevent Alzheimer's disease. Existing biochemical studies conflict on the
Osenkowski, Pamela +8 more
openaire +6 more sources
Tropomyosin Positions in Regulated Thin Filaments Revealed by Cryoelectron Microscopy [PDF]
Past attempts to detect tropomyosin in electron micrograph images of frozen-hydrated troponin-regulated thin filaments under relaxing conditions have not been successful. This raised the possibility that tropomyosin may be disordered on filaments in the off-state, a possibility at odds with the steric blocking model of muscle regulation.
Xu, C. +4 more
openaire +4 more sources
Fabrication of Monolayer Graphene-Coated Grids for Cryoelectron Microscopy. [PDF]
Cryogenic electron microscopy (cryoEM) has emerged as a powerful technique for probing the atomic structure of macromolecular complexes. Sample preparation for cryoEM requires preserving specimens in a thin layer of vitreous ice, typically suspended within the holes of a fenestrated support film. However, all commonly used sample preparation approaches
Basanta B, Chen W, Pride DE, Lander GC.
europepmc +3 more sources
What is in the black box? - A perspective on software in cryoelectron microscopy. [PDF]
This article bemoans the demise of truly modular open-source image processing systems, such as SPIDER, in recent years' development of tools for three-dimensional reconstruction in cryo-electron microscopy. Instead, today's users have to rely on the functionality of software systems that have little or no transparency.
Maji S, Frank J.
europepmc +3 more sources
Structure of the AAVhu.37 capsid by cryoelectron microscopy. [PDF]
Adeno-associated viruses (AAVs) are used as in vivo gene-delivery vectors in gene-therapy products and have been heavily investigated for numerous indications. Over 100 naturally occurring AAV serotypes and variants have been isolated from primate samples.
Kaelber JT +6 more
europepmc +4 more sources
RNA packaging and uncoating in simple single-stranded RNA viruses [PDF]
Simple (non-enveloped) small, positive-sense single-stranded RNA viruses infect hosts from all kingdoms of life. However, their assembly and uncoating processes remain poorly understood. For turnip crinkle virus (TCV), 3D reconstructions by cryoelectron
Bakker, Saskia
core +6 more sources
Artificial Intelligence in Cryo-Electron Microscopy
Cryo-electron microscopy (cryo-EM) has become an unrivaled tool for determining the structure of macromolecular complexes. The biological function of macromolecular complexes is inextricably tied to the flexibility of these complexes.
Jeong Min Chung +2 more
doaj +1 more source

