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Open data
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Basic information
Entry | Database: PDB / ID: 8byv | ||||||
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Title | Cryo-EM structure of a Staphylococus aureus 30S-RbfA complex | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bikmullin, A.G. / Fatkhullin, B. / Stetsenko, A. / Guskov, A. / Yusupov, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural characteristic of RbfA from S. aureus Authors: Bikmullin, A.G. / Fatkhullin, B. / Nurullina, L. / Garaeva, N. / Klochkova, E. / Guskov, A. / Stetsenko, A. / Khusainov, I. / Golubev, A. / Gabdulkhakov, A. / Trachtman, N. / Blokhin, D. / ...Authors: Bikmullin, A.G. / Fatkhullin, B. / Nurullina, L. / Garaeva, N. / Klochkova, E. / Guskov, A. / Stetsenko, A. / Khusainov, I. / Golubev, A. / Gabdulkhakov, A. / Trachtman, N. / Blokhin, D. / Validov, S. / Usachev, K. / Yusupov, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 1016.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 16334MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-30S ribosomal protein ... , 19 types, 19 molecules bcdefghijklmnopqrst
#2: Protein | ![]() Mass: 29136.369 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FZ25 |
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#3: Protein | ![]() Mass: 24143.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW12 |
#4: Protein | ![]() Mass: 23051.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FXK6 |
#5: Protein | ![]() Mass: 17770.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW23 |
#6: Protein | ![]() Mass: 11613.146 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2G113 |
#7: Protein | ![]() Mass: 17826.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P48940 |
#8: Protein | ![]() Mass: 14854.315 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW20 |
#9: Protein | ![]() Mass: 14856.987 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW39 |
#10: Protein | ![]() Mass: 11600.520 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q931G5 |
#11: Protein | ![]() Mass: 13907.978 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW31 |
#12: Protein | ![]() Mass: 15320.870 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P0A0H0 |
#13: Protein | ![]() Mass: 13747.919 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW30 |
#14: Protein | ![]() Mass: 7317.769 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW19 |
#15: Protein | ![]() Mass: 10634.330 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2G2Q1 |
#16: Protein | ![]() Mass: 10253.886 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FZ45 |
#17: Protein | ![]() Mass: 10196.888 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW15 |
#18: Protein | ![]() Mass: 9332.018 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2G111 |
#19: Protein | ![]() Mass: 10639.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FW10 |
#20: Protein | ![]() Mass: 9039.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: Q2FXY6 |
-RNA chain / Protein , 2 types, 2 molecules aA
#1: RNA chain | ![]() Mass: 500464.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: ![]() |
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#21: Protein | Mass: 13535.722 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: rbfA, SAOUHSC_01247 / Production host: ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: ![]() |
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Sample preparation
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Molecular weight | Experimental value: NO | ||||||||||||||||||||||||
Source (natural) |
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Source (recombinant) | Organism: ![]() ![]() ![]() | ||||||||||||||||||||||||
Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() | ||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||||||
Vitrification![]() | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Microscopy | Model: FEI TALOS ARCTICA |
Electron gun | Electron source![]() ![]() |
Electron lens | Mode: BRIGHT FIELD![]() |
Image recording | Electron dose: 53.3 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
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Processing
Software |
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EM software | Name: EPU / Category: image acquisition | |||||||||
CTF correction![]() | Type: NONE | |||||||||
3D reconstruction![]() | Resolution: 2.89 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 81421 / Symmetry type: POINT | |||||||||
Refinement | Cross valid method: NONE |