+Open data
-Basic information
Entry | Database: PDB / ID: 2f4y | ||||||
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Title | Barnase cross-linked with glutaraldehyde | ||||||
Components | Ribonuclease | ||||||
Keywords | HYDROLASE / DENATURATION / LYSOZYME / BARNASE / CROSS-LINKED CRYSTALS / GLUTARALDEHYDE / UREA / THIOUREA / BROMOETHANOL | ||||||
Function / homology | Function and homology information Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters / RNA endonuclease activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | Bacillus amyloliquefaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.15 Å | ||||||
Authors | Prange, T. / Salem, M. | ||||||
Citation | Journal: Biochim.Biophys.Acta / Year: 2006 Title: On the edge of the denaturation process: Application of X-ray diffraction to barnase and lysozyme cross-linked crystals with denaturants in molar concentrations. Authors: Salem, M. / Mauguen, Y. / Prange, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2f4y.cif.gz | 83.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2f4y.ent.gz | 61.6 KB | Display | PDB format |
PDBx/mmJSON format | 2f4y.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f4/2f4y ftp://data.pdbj.org/pub/pdb/validation_reports/f4/2f4y | HTTPS FTP |
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-Related structure data
Related structure data | 2f2nC 2f30C 2f4aC 2f4gC 2f56C 2f5mC 2f5wC 1a2pS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 12199.515 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Plasmid: PMJ1002 / Production host: Escherichia coli (E. coli) References: UniProt: P00648, Hydrolases; Acting on ester bonds; Endoribonucleases producing 3'-phosphomonoesters #2: Chemical | ChemComp-ZN / | #3: 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: 2.25 Å3/Da / Density % sol: 45.39 % |
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Crystal grow | Temperature: 300 K / Method: vapor diffusion, hanging drop / pH: 8 Details: AMMONIUM SULFATE, ZINC CHLORIDE, HEPES BUFFER PROTEIN AT 20MG/ML, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SYNCHROTRON / Site: LURE / Beamline: DW32 / Wavelength: 0.964 / Wavelength: 0.964 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 25, 2002 / Details: CURVATED MULTILAYER MIRROR |
Radiation | Monochromator: CURVATED SI(111) CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.964 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→9 Å / Num. all: 16157 / Num. obs: 14863 / % possible obs: 93.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 4 / Net I/σ(I): 16.3 |
Reflection shell | Resolution: 2.15→2.5 Å / Mean I/σ(I) obs: 7.6 / % possible all: 92.1 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 1A2P Resolution: 2.15→9 Å / Num. parameters: 11548 / Num. restraintsaints: 10675 / σ(F): 2 / Stereochemistry target values: ENGH AND HUBER
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Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 2438 / Occupancy sum non hydrogen: 2862 | |||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→9 Å
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Refine LS restraints |
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