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Yorodumi- PDB-1h0x: Structure of Alba: an archaeal chromatin protein modulated by ace... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1h0x | ||||||
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Title | Structure of Alba: an archaeal chromatin protein modulated by acetylation | ||||||
Components | DNA BINDING PROTEIN SSO10B | ||||||
Keywords | DNA BINDING / ARCHAEA / CHROMATIN / ALBA / ACETYLATION | ||||||
Function / homology | Function and homology information chromosome condensation / chromosome / double-stranded DNA binding / Hydrolases; Acting on ester bonds / RNA binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | SULFOLOBUS SOLFATARICUS (archaea) | ||||||
Method | X-RAY DIFFRACTION / MAD / Resolution: 2.6 Å | ||||||
Authors | Wardleworth, B.N. / Russell, R.J.M. / Bell, S.D. / Taylor, G.L. / White, M.F. | ||||||
Citation | Journal: Embo J. / Year: 2002 Title: Structure of Alba: An Archaeal Chromatin Protein Modulated by Acetylation Authors: Wardleworth, B.N. / Russell, R.J.M. / Bell, S.D. / Taylor, G.L. / White, M.F. #1: Journal: Science / Year: 2002 Title: The Interaction of Alba, a Conserved Archaeal Chromatin Protein, with Sir2 and its Regulation by Acetylation Authors: Bell, S.D. / Botting, C.H. / Wardleworth, B.N. / Jackson, S.P. / White, M.F. #2: Journal: Acta Crystallogr.,Sect.D / Year: 2001 Title: Preliminary Crystallographic Studies of the Double-Stranded DNA Binding Protein Sso10B from Sulfolobus Solfataricus Authors: Wardleworth, B.N. / Russell, R.J.M. / White, M.F. / Taylor, G.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h0x.cif.gz | 46.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h0x.ent.gz | 34.6 KB | Display | PDB format |
PDBx/mmJSON format | 1h0x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h0/1h0x ftp://data.pdbj.org/pub/pdb/validation_reports/h0/1h0x | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.309, 0.413, 0.857), Vector: |
-Components
#1: Protein | Mass: 10990.932 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SULFOLOBUS SOLFATARICUS (archaea) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q97ZF6, UniProt: P60849*PLUS #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: 4.16 Å3/Da / Density % sol: 70 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.50 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: Wardleworth, B.N., (2001) Acta Crystallogr.,Sect.D, 57, 1893. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: MSC / Detector: AREA DETECTOR / Date: Jan 15, 2001 / Details: CONFOCAL |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→30 Å / Num. obs: 10996 / % possible obs: 98 % / Redundancy: 7.6 % / Rmerge(I) obs: 0.046 / Net I/σ(I): 6.9 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 7.6 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 2.7 / % possible all: 95 |
Reflection | *PLUS Lowest resolution: 30 Å / % possible obs: 98 % |
Reflection shell | *PLUS % possible obs: 94.7 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.6→30 Å / Cross valid method: THROUGHOUT
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Refinement step | Cycle: LAST / Resolution: 2.6→30 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 30 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |