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Yorodumi- PDB-6gb8: Copper nitrite reductase from Achromobacter cycloclastes: small c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6gb8 | |||||||||
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Title | Copper nitrite reductase from Achromobacter cycloclastes: small cell polymorph dataset 1 | |||||||||
Components | Copper-containing nitrite reductase | |||||||||
Keywords | OXIDOREDUCTASE / Copper / denitrification / serial synchrotron crystallography / polymorphs / nitrite reductase | |||||||||
Function / homology | Function and homology information denitrification pathway / nitrite reductase (NO-forming) / nitrite reductase (NO-forming) activity / nitrate assimilation / periplasmic space / copper ion binding Similarity search - Function | |||||||||
Biological species | Achromobacter cycloclastes (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.48 Å | |||||||||
Authors | Ebrahim, A. / Appleby, M.V. / Axford, D. / Beale, J. / Moreno-Chicano, T. / Sherrell, D.A. / Strange, R.W. / Owen, R.L. / Hough, M.A. | |||||||||
Funding support | United Kingdom, 2items
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Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2019 Title: Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography. Authors: Ebrahim, A. / Appleby, M.V. / Axford, D. / Beale, J. / Moreno-Chicano, T. / Sherrell, D.A. / Strange, R.W. / Hough, M.A. / Owen, R.L. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6gb8.cif.gz | 81.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6gb8.ent.gz | 59.4 KB | Display | PDB format |
PDBx/mmJSON format | 6gb8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gb/6gb8 ftp://data.pdbj.org/pub/pdb/validation_reports/gb/6gb8 | HTTPS FTP |
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-Related structure data
Related structure data | 6gbbC 6gbyC 6gcgC 5i6kS 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 37059.809 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Achromobacter cycloclastes (bacteria) / Gene: nirK / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P25006, nitrite reductase (NO-forming) | ||||
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#2: Chemical | #3: Chemical | ChemComp-NO2 / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.79 % |
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Crystal grow | Temperature: 298 K / Method: batch mode / pH: 4.5 Details: Batch microcrystals were prepared by rapidly mixing 20 mg/ml AcNiR in 20mM Tris, pH 7.5 with a solution containing 2.5 M ammonium sulphate, 0.1 M sodium citrate pH 4.5 buffer, in a ratio of ...Details: Batch microcrystals were prepared by rapidly mixing 20 mg/ml AcNiR in 20mM Tris, pH 7.5 with a solution containing 2.5 M ammonium sulphate, 0.1 M sodium citrate pH 4.5 buffer, in a ratio of 1:3 and mixed by vortexing for 60 seconds. Microcrystals with a diameter of 5-15 microns grew at room temperature over a period of 4-6 days. |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9686 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 17, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 1.48→29.06 Å / Num. obs: 49882 / % possible obs: 100 % / Redundancy: 548 % / Biso Wilson estimate: 16.6 Å2 / CC1/2: 0.996 / R split: 0.0571 / Net I/σ(I): 1.75 |
Reflection shell | Resolution: 1.48→1.51 Å / Redundancy: 206.5 % / Mean I/σ(I) obs: 0.17 / Num. unique obs: 2471 / CC1/2: 0.726 / R split: 0.8773 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5i6k Resolution: 1.48→29.06 Å / Cor.coef. Fo:Fc: 0.979 / Cor.coef. Fo:Fc free: 0.966 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.076 / ESU R Free: 0.078 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 71.54 Å2 / Biso mean: 22.284 Å2 / Biso min: 12.75 Å2
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Refinement step | Cycle: final / Resolution: 1.48→29.06 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.48→1.518 Å / Total num. of bins used: 20
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