Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy
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Summary
It is established that it is feasible to use cryo-EM to determine near-atomic resolution structures of protein complexes (<500 kDa) with low symmetry, and that the residue-specific radiation damage that occurs with increasing electron dose can be monitored by using dose fractionation tools available with direct electron detector technology.
- Type
- article
- Published
- 2014-07-28
- Cited by
- 191
- References
- 47
- Access
- Open access
- OpenAlex
- https://openalex.org/W1980885982
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:6510634
Keywords
Cryo-electron microscopy, Electron microscope, Resolution (logic), Chemistry, Ion
References
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- Structure and conformational variability of the mycobacterium tuberculosis fatty acid synthase multienzyme complex.
- Heterogeneity of large macromolecular complexes revealed by 3-D cryo-EM variance analysis
- De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy
- Near-atomic resolution using electron cryomicroscopy and single-particle reconstruction
- 3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
- Radiation damage relative to transmission electron microscopy of biological specimens at low temperature: a review
Cited by
- Near-Atomic Resolution Structure Determination of a Cypovirus Capsid and Polymerase Complex Using Cryo-EM at 200kV.
- CryoEM for small molecules discovery, design, understanding and application.
- Validation methods for low-resolution fitting of atomic structures to electron microscopy data
- Cryo-EM: A Unique Tool for the Visualization of Macromolecular Complexity
- The Influence of Frame Alignment with Dose Compensation on the Quality of Single Particle Reconstructions
- Single-particle based helical reconstruction—how to make the most of real and Fourier space
- 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor
- EMRinger: Side-chain-directed model and map validation for 3D Electron Cryomicroscopy
- COMPUTATIONAL METHODOLOGIES for REAL-SPACE STRUCTURAL REFINEMENT of LARGE MACROMOLECULAR COMPLEXES
- Advances in Single-Particle Electron Cryomicroscopy Structure Determination applied to Sub-tomogram Averaging
- Model building and refinement of a natively glycosylated HIV-1 Env protein by high-resolution cryoEM
- Seeing tobacco mosaic virus through direct electron detectors
- 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
- Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports
- Three-Dimensional Reconstruction of Helical Polymers
- Integrative Modeling of Macromolecular Assemblies from Low to Near-Atomic Resolution
- Radiation damage to macromolecules: kill or cure?
- 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy
- Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6
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