Single-particle cryo-EM data acquisition by using direct electron detection camera.
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Summary
How the applications of direct electron detection cameras in cryo-EM have changed the way the data are acquired is discussed.
- Type
- review
- Published
- 2016-02-01
- Cited by
- 50
- References
- 33
- Access
- Open access
- OpenAlex
- https://openalex.org/W2267081965
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24462765
Keywords
Particle (ecology), Data acquisition, Electron, Physics, Computer science
References
- Automatic estimation and correction of anisotropic magnification distortion in electron microscopes.
- Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
- Description and comparison of algorithms for correcting anisotropic magnification in cryo-EM images.
- Alignment of cryo-EM movies of individual particles by optimization of image translations.
- 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor
- Structural determinants of water permeation through aquaporin-1
- Electron microscopy: Ultrastable gold substrates for electron cryomicroscopy.
- Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy.
- Beam-Induced Motion of Vitrified Specimen on Holey Carbon Film
- Paraxial charge compensator for electron cryomicroscopy.
- Movies of ice-embedded particles enhance resolution in electron cryo-microscopy
- A Primer to Single-Particle Cryo-Electron Microscopy
- Alignment of direct detection device micrographs using a robust Optical Flow approach.
- Specimen Charging on Thin Films with One Conducting Layer: Discussion of Physical Principles
- Electron microscopy of gold nanoparticles at atomic resolution
- Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM
- Single-particle cryo-EM at crystallographic resolution
- The Resolution Revolution
- Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures
- Automated molecular microscopy: the new Leginon system.
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- Anisotropic Correction of Beam-induced Motion for Improved Single-particle Electron Cryo-microscopy
- Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo‐electron microscopy
- Structural Study of Heterogeneous Biological Samples by Cryoelectron Microscopy and Image Processing
- Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy.
- MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy
- Dawning of a new era in TRP channel structural biology by cryo-electron microscopy
- Cool views of membrane remodeling
- Structure of an innexin gap junction channel and cryo-EM sample preparation
- Routine Determination of Ice Thickness for Cryo-EM Grids
- Characterization of Hemagglutinin Antigens on Influenza Virus and within Vaccines Using Electron Microscopy
- Cryo-ET bridges the gap between cell biology and structural biophysics
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase
- Challenges and opportunities in cryo-EM single-particle analysis
- Structural Analysis of Arabidopsis thaliana CDC48A ATPase using Single Particle Cryo-Electron Microscopy
- Cross-validation tests for cryo-EM maps using an independent particle set
- Deep-learning with synthetic data enables automated picking of cryo-EM particle images of biological macromolecules
- Developments, applications, and prospects of cryo‐electron microscopy
- Need for Cross-Validation of Single Particle Cryo-EM
- Beyond Protein Structure Determination with MicroED
- Validation tests for cryo-EM maps using an independent particle set