+Open data
-Basic information
Entry | Database: PDB / ID: 1sru | ||||||
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Title | Crystal structure of full length E. coli SSB protein | ||||||
Components | Single-strand binding protein | ||||||
Keywords | REPLICATION | ||||||
Function / homology | Function and homology information single-stranded DNA-binding protein complex / nucleoid / replisome / recombinational repair / positive regulation of catalytic activity / SOS response / mismatch repair / enzyme activator activity / DNA-templated DNA replication / single-stranded DNA binding ...single-stranded DNA-binding protein complex / nucleoid / replisome / recombinational repair / positive regulation of catalytic activity / SOS response / mismatch repair / enzyme activator activity / DNA-templated DNA replication / single-stranded DNA binding / DNA recombination / DNA replication / DNA repair / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD/MAD/molecular replacement / Resolution: 3.3 Å | ||||||
Authors | Savvides, S.N. / Raghunathan, S. / Fuetterer, K. / Kozlov, A.G. / Lohman, T.M. / Waksman, G. | ||||||
Citation | Journal: Protein Sci. / Year: 2004 Title: The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA. Authors: Savvides, S.N. / Raghunathan, S. / Fuetterer, K. / Kozlov, A.G. / Lohman, T.M. / Waksman, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sru.cif.gz | 79.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sru.ent.gz | 58.9 KB | Display | PDB format |
PDBx/mmJSON format | 1sru.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1sru_validation.pdf.gz | 451.6 KB | Display | wwPDB validaton report |
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Full document | 1sru_full_validation.pdf.gz | 478.8 KB | Display | |
Data in XML | 1sru_validation.xml.gz | 19.3 KB | Display | |
Data in CIF | 1sru_validation.cif.gz | 24.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sr/1sru ftp://data.pdbj.org/pub/pdb/validation_reports/sr/1sru | HTTPS FTP |
-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: 12635.293 Da / Num. of mol.: 4 / Fragment: residues 0-112 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: SSB, EXRB, LEXC, B4059, C5049, Z5658, ECS5041, SF4145, S3584 Production host: Escherichia coli (E. coli) / References: UniProt: P02339, UniProt: P0AGE0*PLUS |
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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: 3.69 Å3/Da / Density % sol: 66.66 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG4000, PEG200, Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9879, 0.9794, 0.9792 | ||||||||||||
Detector | Type: CUSTOM-MADE / Detector: CCD | ||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 3.3→20 Å / Num. all: 11620 / Num. obs: 11620 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 | ||||||||||||
Reflection shell | Resolution: 3.3→3.4 Å / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: SAD/MAD/molecular replacement Resolution: 3.3→19.92 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 482092.98 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 102.83 Å2 / ksol: 0.315329 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 102.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.3→19.92 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.3→3.51 Å / Rfactor Rfree error: 0.027 / Total num. of bins used: 6
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: PROTEIN.TOP |