Conformational changes studied by cryo-electron microscopy
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Summary
This review presents a brief summary of the principles and recent advances in macromolecular structure determination by cryo-electron microscopy.
- Type
- review
- Published
- 2000-09-01
- Cited by
- 91
- References
- 30
- OpenAlex
- https://openalex.org/W1533620685
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:20491539
Keywords
Cryo-electron microscopy, Electron microscope, Macromolecule, Crystallography, Resolution (logic)
References
- Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae.
- Structure of α-latrotoxin oligomers reveals that divalent cation-dependent tetramers form membrane pores
- A ratchet-like inter-subunit reorganization of the ribosome during translocation
- Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form.
- GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.
- Three‐dimensional reconstruction from a single‐exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
- A computer-controlled spraying-freezing apparatus for millisecond time-resolution electron cryomicroscopy.
- Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs.
- Reconstruction of Three Dimensional Structures from Electron Micrographs
- Arrangement of tRNAs in pre- and posttranslocational ribosomes revealed by electron cryomicroscopy.
- Quantitative fitting of atomic models into observed densities derived by electron microscopy.
- Situs: A package for docking crystal structures into low-resolution maps from electron microscopy.
- The Escherichia coli large ribosomal subunit at 7.5 A resolution.
- Structure of a human rhinovirus complexed with its receptor molecule.
- Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae.
- Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
- Similarity measures between images
- Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex.
- Acetylcholine receptor channel imaged in the open state
- Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets.
Cited by
- Protein structure dynamics and interplay : by single-particle electron microscopy
- Structure modeling from small angle X-ray scattering data with elastic network normal mode analysis.
- Accurate flexible fitting of high-resolution protein structures into cryo-electron microscopy maps using coarse-grained pseudo-energy minimization.
- Analyzing protein dynamics using hydrogen exchange mass spectrometry.
- Studying microtubules by electron microscopy.
- Integration of biological data: systems, infrastructures and programmable tools
- Cryoelectron tomography of eukaryotic cells.
- Towards unbiased 3D reconstruction : in single-particle cryo-electron microscopy
- The biology of Blumeria effector candidates
- Docking of atomic models into reconstructions from electron microscopy.
- A geometric approach for deciphering protein structure from cryo-em volumes
- Preparation of cells and tissues for immuno EM.
- High resolution transmission electron microscopy of green fluorescent protein
- Consensus among multiple approaches as a reliability measure for flexible fitting into cryo-EM data.
- Femtosecond dynamics of flavoproteins: Charge separation and recombination in riboflavine (vitamin B2)-binding protein and in glucose oxidase enzyme
- Bayesian analysis of individual electron microscopy images: Towards structures of dynamic and heterogeneous biomolecular assemblies
- Comparison of all-atom and coarse-grained normal mode analysis in the elastic network model
- Sequence‐Based Identification of Specific Drug Target Regions in the Thymidylate Synthase Enzyme Family
- Flexible fitting of high-resolution x-ray structures into cryoelectron microscopy maps using biased molecular dynamics simulations.
- Normal-mode flexible fitting of high-resolution structure of biological molecules toward one-dimensional low-resolution data.
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