+Open data
-Basic information
Entry | Database: PDB / ID: 1b8z | ||||||
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Title | HU FROM THERMOTOGA MARITIMA | ||||||
Components | PROTEIN (HISTONELIKE PROTEIN HU) | ||||||
Keywords | DNA BINDING PROTEIN / THERMOTOGA MARITIMA / THERMOSTABLE DNA BINDING PROTEIN | ||||||
Function / homology | Function and homology information chromosome condensation / structural constituent of chromatin / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | Thermotoga maritima (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Christodoulou, E. / Rypniewski, W.R. / Vorgias, C.E. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1998 Title: Cloning, overproduction, purification and crystallization of the DNA binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima. Authors: Christodoulou, E. / Vorgias, C.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b8z.cif.gz | 37.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b8z.ent.gz | 26.8 KB | Display | PDB format |
PDBx/mmJSON format | 1b8z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1b8z_validation.pdf.gz | 414 KB | Display | wwPDB validaton report |
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Full document | 1b8z_full_validation.pdf.gz | 414.1 KB | Display | |
Data in XML | 1b8z_validation.xml.gz | 7.4 KB | Display | |
Data in CIF | 1b8z_validation.cif.gz | 9.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b8/1b8z ftp://data.pdbj.org/pub/pdb/validation_reports/b8/1b8z | 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: 10018.101 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P36206 #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: 2.3 Å3/Da / Density % sol: 46 % | ||||||||||||||||||||
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Crystal grow | pH: 4.6 / Details: pH 4.6 | ||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8833 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Details: MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8833 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→20 Å / Num. obs: 21552 / % possible obs: 99.9 % / Redundancy: 5.9 % / Biso Wilson estimate: 19.82 Å2 / Rsym value: 5.6 / Net I/σ(I): 19.1 |
Reflection shell | Resolution: 1.6→1.63 Å / Mean I/σ(I) obs: 2.7 / Rsym value: 59 / % possible all: 100 |
Reflection | *PLUS Rmerge(I) obs: 0.056 |
Reflection shell | *PLUS % possible obs: 100 % / Rmerge(I) obs: 0.59 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.6→15 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 27.04 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→15 Å
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Refine LS restraints |
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