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Yorodumi- PDB-1pxw: Crystal structure of L7Ae sRNP core protein from Pyrococcus abyssii -
+Open data
-Basic information
Entry | Database: PDB / ID: 1pxw | ||||||
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Title | Crystal structure of L7Ae sRNP core protein from Pyrococcus abyssii | ||||||
Components | LSU ribosomal protein L7AE | ||||||
Keywords | RIBOSOME | ||||||
Function / homology | Function and homology information ribonuclease P activity / tRNA 5'-leader removal / ribosome biogenesis / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / cytoplasm Similarity search - Function | ||||||
Biological species | Pyrococcus abyssi (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.94 Å | ||||||
Authors | Charron, C. / Manival, X. / Charpentier, B. / Branlant, C. / Aubry, A. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2004 Title: Purification, crystallization and preliminary X-ray diffraction data of L7Ae sRNP core protein from Pyrococcus abyssii. Authors: Charron, C. / Manival, X. / Charpentier, B. / Branlant, C. / Aubry, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pxw.cif.gz | 59.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pxw.ent.gz | 44.3 KB | Display | PDB format |
PDBx/mmJSON format | 1pxw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1pxw_validation.pdf.gz | 430.6 KB | Display | wwPDB validaton report |
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Full document | 1pxw_full_validation.pdf.gz | 434 KB | Display | |
Data in XML | 1pxw_validation.xml.gz | 12.6 KB | Display | |
Data in CIF | 1pxw_validation.cif.gz | 17.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/px/1pxw ftp://data.pdbj.org/pub/pdb/validation_reports/px/1pxw | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 14077.445 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus abyssi (archaea) / Production host: Escherichia coli (E. coli) / References: UniProt: P62008 #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: 2.32 Å3/Da / Density % sol: 46.89 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4 Details: PEG MME 2000, magnesium chloride, sodium acetate, pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 8 / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.979 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 20, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.94→15 Å / Num. all: 19168 / Num. obs: 19168 / % possible obs: 95.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.94→2.03 Å / % possible all: 68.6 |
Reflection | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 20 Å / Num. obs: 5958 / % possible obs: 91 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.084 / Num. measured all: 18984 |
Reflection shell | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 3 Å / % possible obs: 77.5 % / Rmerge(I) obs: 0.231 / Mean I/σ(I) obs: 3.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.94→15 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.94→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.94→2.03 Å
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