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| Open AccessDirect visualization of dispersed lipid bicontinuous cubic phases by cryo-electron tomography
Dispersed lipid self-assembly can form various types of particles, including cubosomes, which are useful for drug delivery. Here, Demurtas et al. visualize their three-dimensional structure, showing two continuous water channels separated by lipid bilayers and the mechanism of particle stabilization.
- Davide Demurtas
- , Paul Guichard
- & Laurent Sagalowicz
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| Open AccessLocalized reconstruction of subunits from electron cryomicroscopy images of macromolecular complexes
Electron cryomicroscopy can allow the elucidation of macromolecular structures; however, mismatches in symmetry between different components limit the attainable resolution. Here, the authors set out a computational method for extracting and retaining information from such components.
- Serban L. Ilca
- , Abhay Kotecha
- & Juha T. Huiskonen
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| Open AccessAntibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike
The envelope glycoprotein (Env) trimer is the only antigenic target for broadly neutralizing antibodies on the surface of the HIV-1 virus. Here the authors show that two related monoclonal antibodies bind between gp41 protomers and neutralize HIV-1 by accelerating Env trimer decay.
- Jeong Hyun Lee
- , Daniel P. Leaman
- & Andrew B. Ward
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| Open AccessLarge-volume en-bloc staining for electron microscopy-based connectomics
Large-scale dense reconstruction of neuronal circuits (or connectomics) requires methods for large-volume dense en-blocelectron microscopy (EM) staining. Here the authors develop a protocol for staining tissue blocks from mouse neocortex sized at least 1 mm in diameter, enabling correlated functional and structural circuit analyses.
- Yunfeng Hua
- , Philip Laserstein
- & Moritz Helmstaedter
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| Open AccessCryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution
The Hepatitis C virus (HCV) relies on an internal ribosome entry site (IRES) for translation of all the proteins encoded by its single-stranded RNA genome. Here the authors present a near-atomic cryo-EM structure of the HCV IRES bound to the human ribosome, shedding light on the initiation mechanism of HCV's and related IRESs.
- Nick Quade
- , Daniel Boehringer
- & Nenad Ban
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| Open AccessCryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution
Tailed bacteriophages translocate the genome into and out of the capsid through a portal protein assembly located between the phage s head and tail. Here Sun et al. provide a cryo-EM structure of the bacteriophage T4 portal protein assembly, suggesting the functions and evolution of the portal structure.
- Lei Sun
- , Xinzheng Zhang
- & Michael G. Rossmann
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| Open AccessCryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core
The proteasome is a highly regulated complex fundamental for cell homeostasis and a target for cancer therapy. Here the authors use cryo-EM and single-particle analysis to obtain a detailed map of the interactions between each active sites of the core 20S proteasome and the irreversible inhibitor AdaAhx3L3VS.
- Paula C.A. da Fonseca
- & Edward P. Morris
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| Open AccessGraphene-enabled electron microscopy and correlated super-resolution microscopy of wet cells
Preparing biological material for electron microscopy (EM) involves harsh processing steps that can poorly preserve cellular ultrastructure. Here the authors apply a single layer of graphene onto wet cells to enable direct EM using low voltage, and correlate actin filaments and mitochondria using super-resolution microscopy.
- Michal Wojcik
- , Margaret Hauser
- & Ke Xu
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Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography
While the cytosolic translation machinery is well characterized, the mitochondrial translation system remains largely elusive. Using cryo-electron tomography, Pfeffer et al. describe the ordered organization of mitochondrial polysomes in which each ribosome is tethered to the inner membrane by two defined contacts on the large subunit in situ.
- Stefan Pfeffer
- , Michael W. Woellhaf
- & Friedrich Förster
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Cryo-electron tomography reveals ciliary defects underlying human RSPH1 primary ciliary dyskinesia
Our current understanding of cilia biology and ciliary diseases is incomplete, in part because cilia are hard to visualize. Here, the authors use cryo-electron tomography to image the structure of human cilia with high resolution and uncover the elusive ciliary defects in Primary Ciliary Dyskinesia patients.
- Jianfeng Lin
- , Weining Yin
- & Daniela Nicastro
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High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy
Solving structures of large protein complexes remains a significant challenge for structural biologists. Demers et al. determine the atomic structure of a Shigellatype-III secretion system using a Rosetta-based modelling strategy that draws on both solid-state NMR and cryo-electron microscopy data sets.
- Jean-Philippe Demers
- , Birgit Habenstein
- & Nikolaos G. Sgourakis
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| Open AccessAn atomic model of brome mosaic virus using direct electron detection and real-space optimization
Recent developments in cryo-electron microscopy have enabled structure determination of large protein complexes at almost atomic resolution. Wang et al.combine some of these technologies into an effective workflow, and demonstrate the protocol by solving the atomic structure of an icosahedral RNA virus.
- Zhao Wang
- , Corey F. Hryc
- & Wah Chiu
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| Open AccessVisualizing active membrane protein complexes by electron cryotomography
Few tools are available to identify active membrane proteins within their native lipid environment. Here, Gold et al. report on a strategy that can be used for site-specific labelling of membrane proteins via electron cryotomography.
- Vicki A.M. Gold
- , Raffaele Ieva
- & Werner Kühlbrandt