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Yorodumi- EMDB-1729: 70S Ribosome and Human U4U6U5 tri-snRNP Determined by Cryo-Random... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1729 | |||||||||
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Title | 70S Ribosome and Human U4U6U5 tri-snRNP Determined by Cryo-Random Conical Tilt | |||||||||
Map data | This is a weighted average cryo-RCT structure of human U4U6U5 tri-snRNP. | |||||||||
Sample |
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Keywords | tri-snRNP / wRCT / cryo-RCT | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 30.0 Å | |||||||||
Authors | Sander B / Golas MM / Luhrmann R / Stark H | |||||||||
Citation | Journal: Structure / Year: 2010 Title: An approach for de novo structure determination of dynamic molecular assemblies by electron cryomicroscopy. Authors: Bjoern Sander / Monika M Golas / Reinhard Lührmann / Holger Stark / Abstract: Single-particle electron cryomicroscopy is a powerful method for three-dimensional (3D) structure determination of macromolecular assemblies. Here we address the challenge of determining a 3D ...Single-particle electron cryomicroscopy is a powerful method for three-dimensional (3D) structure determination of macromolecular assemblies. Here we address the challenge of determining a 3D structure in the absence of reference models. The 3D structures are determined by alignment and weighted averaging of densities obtained by native cryo random conical tilt (RCT) reconstructions including consideration of missing data. Our weighted averaging scheme (wRCT) offers advantages for potentially heterogeneous 3D densities of low signal-to-noise ratios. Sets of aligned RCT structures can also be analyzed by multivariate statistical analysis (MSA) to provide insights into snapshots of the assemblies. The approach is used to compute 3D structures of the Escherichia coli 70S ribosome and the human U4/U6.U5 tri-snRNP under vitrified unstained cryo conditions, and to visualize by 3D MSA the L7/L12 stalk of the 70S ribosome and states of tri-snRNP. The approach thus combines de novo 3D structure determination with an analysis of compositional and conformational heterogeneity. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_1729.map.gz | 1.2 MB | EMDB map data format | |
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Header (meta data) | emd-1729-v30.xml emd-1729.xml | 6.3 KB 6.3 KB | Display Display | EMDB header |
Images | 1729.tif | 199.9 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1729 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1729 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_1729.map.gz / Format: CCP4 / Size: 1.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | This is a weighted average cryo-RCT structure of human U4U6U5 tri-snRNP. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Human U4U6U5 tri-snRNP
Entire | Name: Human U4U6U5 tri-snRNP |
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Components |
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-Supramolecule #1000: Human U4U6U5 tri-snRNP
Supramolecule | Name: Human U4U6U5 tri-snRNP / type: sample / ID: 1000 / Details: The sample was monodisperse / Number unique components: 1 |
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-Supramolecule #1: U4U6U5 tri-snRNP
Supramolecule | Name: U4U6U5 tri-snRNP / type: organelle_or_cellular_component / ID: 1 / Name.synonym: tri-snRNP / Recombinant expression: No |
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Source (natural) | Organism: Homo sapiens (human) / synonym: Human / Cell: HeLa / Organelle: Nucleus |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Vitrification | Cryogen name: ETHANE / Instrument: OTHER |
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-Electron microscopy
Microscope | FEI/PHILIPS CM200FEG |
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Electron beam | Acceleration voltage: 160 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2 mm |
Sample stage | Specimen holder: Eucentric / Specimen holder model: GATAN LIQUID NITROGEN |
-Image processing
CTF correction | Details: Each particle |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 30.0 Å / Resolution method: OTHER |