+Open data
-Basic information
Entry | Database: PDB / ID: 1hjp | ||||||
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Title | HOLLIDAY JUNCTION BINDING PROTEIN RUVA FROM E. COLI | ||||||
Components | RUVA | ||||||
Keywords | DNA RECOMBINATION / DNA REPAIR / HOLLIDAY JUNCTION BINDING | ||||||
Function / homology | Function and homology information Holliday junction helicase complex / Holliday junction resolvase complex / four-way junction helicase activity / recombinational repair / SOS response / four-way junction DNA binding / response to radiation / ATP binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2.5 Å | ||||||
Authors | Nishino, T. / Ariyoshi, M. / Iwasaki, H. / Shinagawa, H. / Morikawa, K. | ||||||
Citation | Journal: Structure / Year: 1998 Title: Functional Analyses of the Domain Structure in the Holliday Junction Binding Protein Ruva Authors: Nishino, T. / Ariyoshi, M. / Iwasaki, H. / Shinagawa, H. / Morikawa, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hjp.cif.gz | 46.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hjp.ent.gz | 33.8 KB | Display | PDB format |
PDBx/mmJSON format | 1hjp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hj/1hjp ftp://data.pdbj.org/pub/pdb/validation_reports/hj/1hjp | 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: 22111.668 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cell line: BL21 / Gene: RUVA / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P0A809 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 4 |
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-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.9 Details: 50MM CITRATE PH4.9 500MM NACL 10% GLYCEROL 3% PEG2000 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 4.8 / Method: microdialysis | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6B / Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jun 29, 1996 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→80 Å / Num. obs: 7922 / % possible obs: 93.7 % / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 8.4 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.85 / Mean I/σ(I) obs: 1.9 / % possible all: 80.5 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2.5→15 Å / Cross valid method: FREE R / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.5→15 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 7873 / Rfactor all: 0.229 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |