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Open data
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Basic information
Entry | ![]() | ||||||||||||||||||
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Title | 70S initiation complex (tRNA-fMet M1 + UUG start codon) | ||||||||||||||||||
![]() | Masked, sharpened map from homogeneous 3D refinement (sharpening B factor of -63.7 A^2), used for modeling | ||||||||||||||||||
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![]() | translation initiation / tRNA-fMet M1 / frameshifting / ribosome | ||||||||||||||||||
Function / homology | ![]() DnaA-L2 complex / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / transcription antitermination / DNA-templated transcription termination / response to radiation ...DnaA-L2 complex / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / transcription antitermination / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / response to antibiotic / mRNA binding / RNA binding / zinc ion binding / metal ion binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.59 Å | ||||||||||||||||||
![]() | Mattingly JM / Nguyen HA / Dunham CM | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural analysis of noncanonical translation initiation complexes. Authors: Mattingly JM / Nguyen HA / Roy B / Fredrick K / Dunham CM | ||||||||||||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 230.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 82.3 KB 82.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.1 KB | Display | ![]() |
Images | ![]() | 226.9 KB | ||
Masks | ![]() | 244.1 MB | ![]() | |
Filedesc metadata | ![]() | 16 KB | ||
Others | ![]() ![]() ![]() ![]() | 123 MB 182 MB 226.9 MB 226.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 22.3 KB | Display | |
Data in CIF | ![]() | 28.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9cg5MC ![]() 9ax7C ![]() 9ax8C ![]() 9cg6C ![]() 9cg7C C: citing same article ( M: atomic model generated by this map |
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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 | Masked, sharpened map from homogeneous 3D refinement (sharpening B factor of -63.7 A^2), used for modeling | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.045 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : 70S initiation complex (tRNA-fMet M1 + UUG start codon)
+Supramolecule #1: 70S initiation complex (tRNA-fMet M1 + UUG start codon)
+Macromolecule #1: 50S ribosomal protein L33
+Macromolecule #2: 50S ribosomal protein L34
+Macromolecule #3: 50S ribosomal protein L35
+Macromolecule #4: 50S ribosomal protein L36
+Macromolecule #5: 50S ribosomal protein L31
+Macromolecule #7: 30S ribosomal protein S2
+Macromolecule #8: 30S ribosomal protein S3
+Macromolecule #9: 30S ribosomal protein S4
+Macromolecule #10: 30S ribosomal protein S5
+Macromolecule #11: 30S ribosomal protein S6
+Macromolecule #12: 30S ribosomal protein S7
+Macromolecule #13: 30S ribosomal protein S8
+Macromolecule #14: 30S ribosomal protein S9
+Macromolecule #15: 30S ribosomal protein S10
+Macromolecule #16: 30S ribosomal protein S11
+Macromolecule #17: 30S ribosomal protein S12
+Macromolecule #18: 30S ribosomal protein S13
+Macromolecule #19: 30S ribosomal protein S14
+Macromolecule #20: 30S ribosomal protein S15
+Macromolecule #21: 30S ribosomal protein S16
+Macromolecule #22: 30S ribosomal protein S17
+Macromolecule #23: 30S ribosomal protein S18
+Macromolecule #24: 30S ribosomal protein S19
+Macromolecule #25: 30S ribosomal protein S20
+Macromolecule #26: 30S ribosomal protein S21
+Macromolecule #31: 50S ribosomal protein L2
+Macromolecule #32: 50S ribosomal protein L3
+Macromolecule #33: 50S ribosomal protein L4
+Macromolecule #34: 50S ribosomal protein L5
+Macromolecule #35: 50S ribosomal protein L6
+Macromolecule #36: 50S ribosomal protein L9
+Macromolecule #37: 50S ribosomal protein L13
+Macromolecule #38: 50S ribosomal protein L14
+Macromolecule #39: 50S ribosomal protein L15
+Macromolecule #40: 50S ribosomal protein L16
+Macromolecule #41: 50S ribosomal protein L17
+Macromolecule #42: 50S ribosomal protein L18
+Macromolecule #43: 50S ribosomal protein L19
+Macromolecule #44: 50S ribosomal protein L20
+Macromolecule #45: 50S ribosomal protein L21
+Macromolecule #46: 50S ribosomal protein L22
+Macromolecule #47: 50S ribosomal protein L23
+Macromolecule #48: 50S ribosomal protein L24
+Macromolecule #49: 50S ribosomal protein L25
+Macromolecule #50: 50S ribosomal protein L27
+Macromolecule #51: 50S ribosomal protein L28
+Macromolecule #52: 50S ribosomal protein L29
+Macromolecule #53: 50S ribosomal protein L30
+Macromolecule #54: 50S ribosomal protein L32
+Macromolecule #6: 16S ribosomal RNA
+Macromolecule #27: mRNA
+Macromolecule #28: P-site tRNA-fMet M1
+Macromolecule #29: 23S ribosomal RNA
+Macromolecule #30: 5S ribosomal RNA
+Macromolecule #55: ZINC ION
+Macromolecule #56: MAGNESIUM ION
+Macromolecule #57: BETA-L-ASPARTIC ACID
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: C-flat-1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 1 / Number real images: 2441 / Average electron dose: 58.4 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 79000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | PDB ID: Chain - Source name: PDB / Chain - Initial model type: experimental model |
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Details | Starting model was fit into the unsharpened 3D reconstruction in UCSF ChimeraX before performing real-space refinement with the sharpened map in PHENIX |
Refinement | Space: REAL / Protocol: FLEXIBLE FIT / Overall B value: 63.7 |
Output model | ![]() PDB-9cg5: |