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Yorodumi- PDB-5m7k: Blastochloris viridis photosynthetic reaction center - RC_vir_xfel -
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Open data
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Basic information
| Entry | Database: PDB / ID: 5m7k | ||||||
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| Title | Blastochloris viridis photosynthetic reaction center - RC_vir_xfel | ||||||
Components |
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Keywords | PHOTOSYNTHESIS / Photosynthetic / Reaction Center | ||||||
| Function / homology | Function and homology informationplasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / : / photosynthesis, light reaction / photosynthesis / electron transfer activity / iron ion binding / heme binding / metal ion binding Similarity search - Function | ||||||
| Biological species | Blastochloris viridis (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / FREE ELECTRON LASER / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | ||||||
Authors | Sharma, A.S. / Johansson, L. / Dunevall, E. / Wahlgren, W.Y. / Neutze, R. / Katona, G. | ||||||
Citation | Journal: Acta Crystallogr A Found Adv / Year: 2017Title: Asymmetry in serial femtosecond crystallography data. Authors: Sharma, A. / Johansson, L. / Dunevall, E. / Wahlgren, W.Y. / Neutze, R. / Katona, G. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5m7k.cif.gz | 273.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5m7k.ent.gz | 211.5 KB | Display | PDB format |
| PDBx/mmJSON format | 5m7k.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5m7k_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 5m7k_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 5m7k_validation.xml.gz | 48 KB | Display | |
| Data in CIF | 5m7k_validation.cif.gz | 61.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m7/5m7k ftp://data.pdbj.org/pub/pdb/validation_reports/m7/5m7k | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5m7jC ![]() 5m7lC ![]() 4casS S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
-Protein , 1 types, 1 molecules A
| #1: Protein | Mass: 39419.176 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Blastochloris viridis (bacteria) / References: UniProt: P07173 |
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-Reaction center protein ... , 3 types, 3 molecules BCD
| #2: Protein | Mass: 30600.299 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Blastochloris viridis (bacteria) / References: UniProt: P06009 |
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| #3: Protein | Mass: 36063.383 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Blastochloris viridis (bacteria) / References: UniProt: P06010 |
| #4: Protein | Mass: 28557.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Blastochloris viridis (bacteria) / References: UniProt: P06008 |
-Non-polymers , 10 types, 20 molecules 


















| #5: Chemical | ChemComp-HEC / #6: Chemical | ChemComp-DGA / | #7: Chemical | ChemComp-BCL / #8: Chemical | #9: Chemical | #10: Chemical | ChemComp-FE2 / | #11: Chemical | ChemComp-MQ7 / | #12: Chemical | ChemComp-NS5 / | #13: Chemical | ChemComp-OTP / ( | #14: Chemical | |
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-Details
| Has protein modification | Y |
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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: 3.62 Å3/Da / Density % sol: 65.98 % |
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| Crystal grow | Temperature: 293 K / Method: batch mode Details: Melted monoolein was thoroughly mixed in a ratio of 3:2 (v/v) with 0.1M HEPES, pH 7.5, 0.1 % LDAO until a viscous, transparent LCP was obtained. The formed phase was then transferred into a ...Details: Melted monoolein was thoroughly mixed in a ratio of 3:2 (v/v) with 0.1M HEPES, pH 7.5, 0.1 % LDAO until a viscous, transparent LCP was obtained. The formed phase was then transferred into a glass vial and sponge-phase-inducing solution (1:4 ratio) was added containing 16% Jeffamine M-600, 1M HEPES pH 7.9, 0.7 M Ammonium sulphate, 2.5% 1,2,3-Heptanetriol, which swell the cubic phase to sponge phase. After phase separation overnight, the upper phase (sponge phase) was harvested. Crystals were grown using batch crystallization in the lipidic-sponge phase. Equal amount of sponge phase and protein were mixed with 2/5 (v/v) of 1.2 M Tris-sodium citrate and allowed to incubate for several weeks. |
-Data collection
| Diffraction | Mean temperature: 293 K / Serial crystal experiment: Y |
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| Diffraction source | Source: FREE ELECTRON LASER / Site: SLAC LCLS / Beamline: CXI / Wavelength: 1.32 Å |
| Detector | Type: CS-PAD CXI-1 / Detector: PIXEL / Date: Feb 19, 2011 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.32 Å / Relative weight: 1 |
| Reflection | Resolution: 3.5→58 Å / Num. obs: 25004 / % possible obs: 99.4 % / Redundancy: 59 % / Net I/σ(I): 3.5 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 4CAS Resolution: 3.5→55.438 Å / SU ML: 0.47 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 23.3
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.5→55.438 Å
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| Refine LS restraints |
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| LS refinement shell |
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Blastochloris viridis (bacteria)
X-RAY DIFFRACTION
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