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Open data
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Basic information
Entry | ![]() | |||||||||||||||||||||
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Title | PAO1 wild-type ribosome, R, reference map | |||||||||||||||||||||
![]() | PAO1 wild-type ribosome, R, reference map | |||||||||||||||||||||
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![]() | Ribosome / PAO1 / wild type / antibiotic resistance | |||||||||||||||||||||
Function / homology | ![]() transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit ...transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S 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 / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.46 Å | |||||||||||||||||||||
![]() | Mesa P / Montoya G | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Detuning of the Ribosome Conformational Landscape Promotes Antibiotic Resistance and Collateral Sensitivity. Authors: Mesa P / Jimenez-Fernandez A / La Rosa R / Espinosa-Portero R / Johansen HK / Molin S / Montoya G | |||||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 136.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 72.3 KB 72.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 17.6 KB | Display | ![]() |
Images | ![]() | 185.2 KB | ||
Filedesc metadata | ![]() | 13.6 KB | ||
Others | ![]() ![]() | 138.9 MB 138.9 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 | ![]() | 22.1 KB | Display | |
Data in CIF | ![]() | 29.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8rwgMC ![]() 19609 ![]() 19610 ![]() 19611 ![]() 19615 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 | PAO1 wild-type ribosome, R, reference map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.832 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: R half map 2
File | emd_19547_half_map_1.map | ||||||||||||
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Annotation | R half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: R half map 1
File | emd_19547_half_map_2.map | ||||||||||||
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Annotation | R half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : PAO1 wild-type ribosome
+Supramolecule #1: PAO1 wild-type ribosome
+Macromolecule #1: 50S ribosomal protein L27
+Macromolecule #2: 50S ribosomal protein L28
+Macromolecule #3: 50S ribosomal protein L29
+Macromolecule #4: 50S ribosomal protein L30
+Macromolecule #5: 50S ribosomal protein L32
+Macromolecule #6: Large ribosomal subunit protein bL33
+Macromolecule #7: 50S ribosomal protein L34
+Macromolecule #8: 50S ribosomal protein L35
+Macromolecule #9: 50S ribosomal protein L36
+Macromolecule #13: 50S ribosomal protein L2
+Macromolecule #14: 50S ribosomal protein L3
+Macromolecule #15: 50S ribosomal protein L4
+Macromolecule #16: 50S ribosomal protein L5
+Macromolecule #17: 50S ribosomal protein L6
+Macromolecule #18: 50S ribosomal protein L9
+Macromolecule #19: 50S ribosomal protein L13
+Macromolecule #20: 50S ribosomal protein L14
+Macromolecule #21: 50S ribosomal protein L15
+Macromolecule #22: 50S ribosomal protein L16
+Macromolecule #23: 50S ribosomal protein L17
+Macromolecule #24: 50S ribosomal protein L18
+Macromolecule #25: 50S ribosomal protein L19
+Macromolecule #26: 50S ribosomal protein L20
+Macromolecule #27: 50S ribosomal protein L21
+Macromolecule #28: Large ribosomal subunit protein uL22
+Macromolecule #29: 50S ribosomal protein L23
+Macromolecule #30: 50S ribosomal protein L24
+Macromolecule #31: 50S ribosomal protein L25
+Macromolecule #32: 30S ribosomal protein S2
+Macromolecule #33: 30S ribosomal protein S3
+Macromolecule #34: 30S ribosomal protein S4
+Macromolecule #35: 30S ribosomal protein S5
+Macromolecule #36: 30S ribosomal protein S6
+Macromolecule #37: 30S ribosomal protein S7
+Macromolecule #38: 30S ribosomal protein S8
+Macromolecule #39: 30S ribosomal protein S9
+Macromolecule #40: 30S ribosomal protein S10
+Macromolecule #41: 30S ribosomal protein S11
+Macromolecule #42: 30S ribosomal protein S12
+Macromolecule #43: 30S ribosomal protein S13
+Macromolecule #44: 30S ribosomal protein S14
+Macromolecule #45: 30S ribosomal protein S15
+Macromolecule #46: 30S ribosomal protein S16
+Macromolecule #47: 30S ribosomal protein S17
+Macromolecule #48: 30S ribosomal protein S18
+Macromolecule #49: 30S ribosomal protein S19
+Macromolecule #50: 30S ribosomal protein S20
+Macromolecule #51: 30S ribosomal protein S21
+Macromolecule #10: 23S ribosomal RNA
+Macromolecule #11: 16S ribosomal RNA
+Macromolecule #12: 5S ribosomal RNA
+Macromolecule #52: ZINC ION
+Macromolecule #53: MAGNESIUM ION
+Macromolecule #54: water
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1 mg/mL | |||||||||||||||
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Buffer | pH: 7.6 Component:
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Vitrification | Cryogen name: NITROGEN / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 3773 / Average exposure time: 50.0 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 96000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |