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Open data
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Basic information
Entry | Database: PDB / ID: 1an7 | ||||||
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Title | RIBOSOMAL PROTEIN S8 FROM THERMUS THERMOPHILUS | ||||||
![]() | RIBOSOMAL PROTEIN S8 | ||||||
![]() | RIBOSOMAL PROTEIN / RRNA-PROTEIN BINDING / PROTEIN-PROTEIN BINDING / THERMUS THERMOPHILUS | ||||||
Function / homology | ![]() cytosolic small ribosomal subunit / rRNA binding / structural constituent of ribosome / translation Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nevskaya, N. / Nikonov, S. / Al-Karadaghi, S. | ||||||
![]() | ![]() Title: Crystal structure of ribosomal protein S8 from Thermus thermophilus reveals a high degree of structural conservation of a specific RNA binding site. Authors: Nevskaya, N. / Tishchenko, S. / Nikulin, A. / al-Karadaghi, S. / Liljas, A. / Ehresmann, B. / Ehresmann, C. / Garber, M. / Nikonov, S. #1: ![]() Title: Crystallization and Preliminary Crystallographic Analysis of Ribosomal Protein S8 from Thermus Thermophilus Authors: Tishchenko, S.V. / Vysotskaya, V.S. / Fomenkova, N.P. / Nikonov, S.V. / Ehresmann, B. / Garber, M.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.3 KB | Display | ![]() |
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PDB format | ![]() | 49.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.3 KB | Display | ![]() |
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Full document | ![]() | 430.5 KB | Display | |
Data in XML | ![]() | 12.5 KB | Display | |
Data in CIF | ![]() | 15.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.8928, 0.0842, -0.4425), Vector: |
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Components
#1: Protein | Mass: 15624.214 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 60 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | ||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 24 ℃ / Method: vapor diffusion, hanging dropDetails: Tishchenko, S.V., (1997) Proteins: Struct.,Funct., Genet., 27, 309. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Feb 10, 1996 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→20 Å / Num. obs: 8932 / % possible obs: 94.5 % / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 33.6 Å2 / Rmerge(I) obs: 0.051 |
Reflection shell | Resolution: 2.9→2.95 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.019 / % possible all: 93.6 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 37 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→8 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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