+Open data
-Basic information
Entry | Database: PDB / ID: 1bxe | ||||||
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Title | RIBOSOMAL PROTEIN L22 FROM THERMUS THERMOPHILUS | ||||||
Components | PROTEIN (RIBOSOMAL PROTEIN L22) | ||||||
Keywords | RNA BINDING PROTEIN / RIBOSOMAL PROTEIN / PROTEIN SYNTHESIS / RNA BINDING / ANTIBIOTICS RESISTANCE | ||||||
Function / homology | Function and homology information large ribosomal subunit / rRNA binding / structural constituent of ribosome / translation Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 1.9 Å | ||||||
Authors | Unge, J. / Aberg, A. / Al-Karadaghi, S. / Nikulin, A. / Nikonov, S. / Davydova, N. / Nevskaya, N. / Garber, M. / Liljas, A. | ||||||
Citation | Journal: Structure / Year: 1998 Title: The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistance. Authors: Unge, J. / berg, A. / Al-Kharadaghi, S. / Nikulin, A. / Nikonov, S. / Davydova, N. / Nevskaya, N. / Garber, M. / Liljas, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bxe.cif.gz | 31 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bxe.ent.gz | 23.5 KB | Display | PDB format |
PDBx/mmJSON format | 1bxe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bx/1bxe ftp://data.pdbj.org/pub/pdb/validation_reports/bx/1bxe | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 12901.846 Da / Num. of mol.: 1 / Mutation: MET1MSE, MET64MSE Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Cellular location: RIBOSOME / Production host: Escherichia coli (E. coli) / References: UniProt: P48286 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.83 Å3/Da / Density % sol: 56.5 % | |||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7 | |||||||||||||||
Crystal grow | *PLUS pH: 4.5 / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 1.012 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.012 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 12173 / % possible obs: 98 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Rmerge(I) obs: 0.053 |
Reflection shell | Resolution: 1.9→1.93 Å / Rmerge(I) obs: 0.159 / % possible all: 94.8 |
Reflection shell | *PLUS % possible obs: 94.8 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 1.9→10 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 20.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.99 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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