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Yorodumi- PDB-3tj1: Crystal Structure of RNA Polymerase I Transcription Initiation Fa... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 3tj1 | ||||||
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| Title | Crystal Structure of RNA Polymerase I Transcription Initiation Factor Rrn3 | ||||||
Components | RNA polymerase I-specific transcription initiation factor RRN3 | ||||||
Keywords | TRANSCRIPTION / HEAT repeat / Transcription Factor / Nucleus | ||||||
| Function / homology | Function and homology informationRNA polymerase I core binding / RNA polymerase I general transcription initiation factor activity / RNA polymerase I general transcription initiation factor binding / rDNA binding / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / transcription initiation at RNA polymerase I promoter / nucleolus / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.85 Å | ||||||
Authors | Blattner, C. / Jennebach, S. / Herzog, F. / Mayer, A. / Cheung, A.C.M. / Witte, G. / Lorenzen, K. / Hopfner, K.-P. / Heck, A.J.R. / Aebersold, R. / Cramer, P. | ||||||
Citation | Journal: Genes Dev. / Year: 2011Title: Molecular basis of Rrn3-regulated RNA polymerase I initiation and cell growth. Authors: Blattner, C. / Jennebach, S. / Herzog, F. / Mayer, A. / Cheung, A.C. / Witte, G. / Lorenzen, K. / Hopfner, K.P. / Heck, A.J. / Aebersold, R. / Cramer, P. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3tj1.cif.gz | 409 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3tj1.ent.gz | 338.2 KB | Display | PDB format |
| PDBx/mmJSON format | 3tj1.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tj/3tj1 ftp://data.pdbj.org/pub/pdb/validation_reports/tj/3tj1 | HTTPS FTP |
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-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 74831.883 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RRN3, YKL125W / Plasmid: pET28 / Production host: ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 53.85 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 14% PEG 3350, 250 mM sodium-potassium-tartrate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
| Diffraction | Mean temperature: 100 K | ||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.0086, 1.0094, 1.0129 | ||||||||||||
| Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 22, 2008 | ||||||||||||
| Radiation | Monochromator: Liquid nitrogen cooled channel-cut silicon monochromator Si(111) Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
| Radiation wavelength |
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| Reflection | Resolution: 2.85→50 Å / Num. all: 38079 / Num. obs: 38054 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 | ||||||||||||
| Reflection shell | Resolution: 2.85→2.92 Å / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MAD / Resolution: 2.85→48.55 Å / Cor.coef. Fo:Fc: 0.9308 / Cor.coef. Fo:Fc free: 0.9165 / SU R Cruickshank DPI: 0.701 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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| Displacement parameters | Biso mean: 62.5 Å2
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| Refine analyze | Luzzati coordinate error obs: 0.436 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.85→48.55 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.85→2.93 Å / Total num. of bins used: 19
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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