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Yorodumi- PDB-5crx: ASYMMETRIC DNA-BENDING IN THE CRE-LOXP SITE-SPECIFIC RECOMBINATIO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5crx | ||||||
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Title | ASYMMETRIC DNA-BENDING IN THE CRE-LOXP SITE-SPECIFIC RECOMBINATION SYNAPSE | ||||||
Components |
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Keywords | PROTEIN/DNA / CRE RECOMBINASE / DNA BENDING / SITE SPECIFIC RECOMBINATION / PROTEIN-DNA INTERACTION / PROTEIN-DNA complex | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Enterobacteria phage P1 (virus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Guo, F. / Gopaul, D.N. / Van Duyne, G.D. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1999 Title: Asymmetric DNA bending in the Cre-loxP site-specific recombination synapse. Authors: Guo, F. / Gopaul, D.N. / Van Duyne, G.D. #1: Journal: Embo J. / Year: 1998 Title: Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination. Authors: Gopaul, D.N. / Guo, F. / Van Duyne, G.D. #2: Journal: Nature / Year: 1997 Title: Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. Authors: Guo, F. / Gopaul, D.N. / van Duyne, G.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5crx.cif.gz | 174.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5crx.ent.gz | 133.6 KB | Display | PDB format |
PDBx/mmJSON format | 5crx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cr/5crx ftp://data.pdbj.org/pub/pdb/validation_reports/cr/5crx | HTTPS FTP |
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-Related structure data
Related structure data | 4crxC 1crxS 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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Unit cell |
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-Components
#1: DNA chain | Mass: 10759.968 Da / Num. of mol.: 2 / Source method: obtained synthetically #2: Protein | Mass: 38579.164 Da / Num. of mol.: 2 / Mutation: Y324F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage P1 (virus) / Genus: P1-like viruses / Gene: CRE / Plasmid: PET21A / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASMIC / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P06956 #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: 2.97 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5 / Details: pH 5.0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 5.6 / Method: vapor diffusion, hanging 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: CHESS / Beamline: F2 / Wavelength: 0.9188 |
Detector | Type: ADSC / Detector: CCD / Date: Dec 1, 1997 / Details: MIRRORS |
Radiation | Monochromator: SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9188 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→99 Å / Num. obs: 32242 / % possible obs: 97.3 % / Observed criterion σ(I): -3 / Redundancy: 4.8 % / Biso Wilson estimate: 63.4 Å2 / Rsym value: 0.069 / Net I/σ(I): 12.59 |
Reflection shell | Resolution: 2.7→2.78 Å / Redundancy: 3.71 % / Mean I/σ(I) obs: 23.76 / Rsym value: 0.23 / % possible all: 93.9 |
Reflection | *PLUS Rmerge(I) obs: 0.066 |
Reflection shell | *PLUS % possible obs: 94 % / Rmerge(I) obs: 0.23 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1CRX Resolution: 2.7→48 Å / Rfactor Rfree error: 0.017 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 50.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→48 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.82 Å / Rfactor Rfree error: 0.02 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 48 Å / σ(F): 2 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 50.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.7 Å / Rfactor Rfree: 0.437 / % reflection Rfree: 5 % / Rfactor Rwork: 0.337 |