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- EMDB-0699: 120kV MicroED structure of FUS (37-42) SYSGYS solved from single ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-0699 | |||||||||||||||
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Title | 120kV MicroED structure of FUS (37-42) SYSGYS solved from single crystal at 0.65 A | |||||||||||||||
![]() | 2Fo-Fc map | |||||||||||||||
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![]() | FUS / MicroED / Ultrahigh resolution / RNA BINDING PROTEIN | |||||||||||||||
Function / homology | ![]() mRNA stabilization / intracellular non-membrane-bounded organelle / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / positive regulation of double-strand break repair via homologous recombination / transcription coregulator activity / mRNA Splicing - Major Pathway / RNA splicing / molecular condensate scaffold activity / mRNA 3'-UTR binding ...mRNA stabilization / intracellular non-membrane-bounded organelle / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / positive regulation of double-strand break repair via homologous recombination / transcription coregulator activity / mRNA Splicing - Major Pathway / RNA splicing / molecular condensate scaffold activity / mRNA 3'-UTR binding / protein homooligomerization / transcription coactivator activity / amyloid fibril formation / chromatin binding / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus / metal ion binding / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | electron crystallography / cryo EM / Resolution: 0.65 Å | |||||||||||||||
![]() | Zhou H / Luo F | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Programming Conventional Electron Microscopes for Solving Ultrahigh-Resolution Structures of Small and Macro-Molecules. Authors: Heng Zhou / Feng Luo / Zhipu Luo / Dan Li / Cong Liu / Xueming Li / ![]() Abstract: Microcrystal electron diffraction (MicroED) is becoming a powerful tool in determining the crystal structures of biological macromolecules and small organic compounds. However, wide applications of ...Microcrystal electron diffraction (MicroED) is becoming a powerful tool in determining the crystal structures of biological macromolecules and small organic compounds. However, wide applications of this technique are still limited by the special requirement for radiation-tolerated movie-mode camera and the lack of automated data collection methods. Herein, we develop a stage-camera synchronization scheme to minimize the hardware requirements and enable the use of the conventional electron cryo-microscope with a single-frame CCD camera, which ensures not only the acquisition of ultrahigh-resolution diffraction data but also low cost in practice. This method renders the structure determination of both peptide and small organic compounds at ultrahigh resolution up to ∼0.60 Å with unambiguous assignment of nearly all hydrogen atoms. The present work provides a widely applicable solution for routine structure determination of MicroED and demonstrates the capability of the low-end 120 kV microscope with a CCD camera in solving ultrahigh resolution structures of both organic compounds and biological macromolecules. | |||||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 12.6 KB 12.6 KB | Display Display | ![]() |
Images | ![]() | 45.2 KB | ||
Filedesc metadata | ![]() | 4.2 KB | ||
Others | ![]() ![]() | 1.6 MB 1.6 MB | ||
Filedesc structureFactors | ![]() | 109.7 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6kj4MC ![]() 0696C ![]() 0697C ![]() 0698C ![]() 6kj1C ![]() 6kj2C ![]() 6kj3C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | 2Fo-Fc map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X: 0.15882 Å / Y: 0.15593 Å / Z: 0.14709 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: Fo-Fc map
File | emd_0699_additional.map | ||||||||||||
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Annotation | Fo-Fc map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Fo-Fc map
File | emd_0699_additional_1.map | ||||||||||||
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Annotation | Fo-Fc map | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : FUS LC RAC1
Entire | Name: FUS LC RAC1 |
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Components |
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-Supramolecule #1: FUS LC RAC1
Supramolecule | Name: FUS LC RAC1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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-Macromolecule #1: RNA-binding protein FUS
Macromolecule | Name: RNA-binding protein FUS / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 662.648 Da |
Sequence | String: SYSGYS UniProtKB: RNA-binding protein FUS |
-Macromolecule #2: water
Macromolecule | Name: water / type: ligand / ID: 2 / Number of copies: 1 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | electron crystallography |
Aggregation state | 3D array |
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Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TECNAI 12 |
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Image recording | Film or detector model: FEI EAGLE (4k x 4k) / Average electron dose: 0.05 e/Å2 |
Electron beam | Acceleration voltage: 120 kV / Electron source: LAB6 |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DIFFRACTION / Camera length: 500 mm |
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Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 0.65 Å / Resolution method: DIFFRACTION PATTERN/LAYERLINES |
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Crystallography statistics | Number intensities measured: 9705 / Number structure factors: 3711 / Fourier space coverage: 63.2 / R sym: 0.217 / R merge: 0.217 / Overall phase error: 32.33 / Overall phase residual: 1 / Phase error rejection criteria: 60 / High resolution: 0.65 Å / Shell - Shell ID: 1 / Shell - High resolution: 0.65 Å / Shell - Low resolution: 0.68 Å / Shell - Number structure factors: 291 / Shell - Phase residual: 1 / Shell - Fourier space coverage: 49.83 / Shell - Multiplicity: 1.86 |
-Atomic model buiding 1
Refinement | Space: RECIPROCAL / Protocol: AB INITIO MODEL |
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Output model | ![]() PDB-6kj4: |