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Mini-Bacterioferritin From Candidatus Methanoperedens Species Blz2 As Isolated Form At 1.07-A Resolution
Organism: Candidatus methanoperedens sp. blz2
Method: X-RAY DIFFRACTION Resolution:1.07 Å Release Date: 2026-04-01 Classification: OXIDOREDUCTASE Ligands: EDO, FE, FEC, MG, NA, GOL |
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Mini-Bacterioferritin From Candidatus Methanoperedens Species Blz2 In A Partially Oxidized State
Organism: Candidatus methanoperedens sp. blz2
Method: X-RAY DIFFRACTION Resolution:1.54 Å Release Date: 2026-04-01 Classification: OXIDOREDUCTASE Ligands: FE, FEC |
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Mini-Bacterioferritin From Candidatus Methanoperedens Species Blz2 Oxidized Then Chemically Reduced
Organism: Candidatus methanoperedens sp. blz2
Method: X-RAY DIFFRACTION Resolution:2.08 Å Release Date: 2026-04-01 Classification: OXIDOREDUCTASE Ligands: FE, FEC |
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Mini-Bacterioferritin From Candidatus Methanoperedens Species Blz2 Untreated Control Of A Redox Cycling Experiment
Organism: Candidatus methanoperedens sp. blz2
Method: X-RAY DIFFRACTION Resolution:1.68 Å Release Date: 2026-04-01 Classification: OXIDOREDUCTASE Ligands: FEC, FE |
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Dimeric State Of The F420-Reducing Hydrogenase From Methanothermococcus Thermolithotrophicus In Crystalline Form 1
Organism: Methanothermococcus thermolithotrophicus dsm 2095
Method: X-RAY DIFFRACTION Resolution:2.30 Å Release Date: 2025-10-22 Classification: OXIDOREDUCTASE Ligands: NFU, NA, SO4, GOL, FE, SF4, FAD, CL, EPE |
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Dimeric State Of The F420-Reducing Hydrogenase From Methanothermococcus Thermolithotrophicus In Crystalline Form 2
Organism: Methanothermococcus thermolithotrophicus dsm 2095
Method: X-RAY DIFFRACTION Resolution:1.65 Å Release Date: 2025-10-22 Classification: OXIDOREDUCTASE Ligands: NFU, GOL, FE, SF4, FAD |
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Dimeric State Of The F420-Reducing Hydrogenase From Methanothermococcus Thermolithotrophicus In Crystalline Form 3
Organism: Methanothermococcus thermolithotrophicus dsm 2095
Method: X-RAY DIFFRACTION Resolution:3.13 Å Release Date: 2025-10-22 Classification: OXIDOREDUCTASE Ligands: GOL, MES, NFU, FE, SO4, EDO, FAD, SF4, PE4, FES |
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Cubic State Of The F420-Reducing Hydrogenase From Methanothermococcus Thermolithotrophicus
Organism: Methanothermococcus thermolithotrophicus dsm 2095
Method: X-RAY DIFFRACTION Resolution:2.85 Å Release Date: 2025-10-22 Classification: OXIDOREDUCTASE Ligands: SO4, NFU, FAD, GOL, SF4 |
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Methyl-Coenzyme M Reductase Of Anme-2D Candidatus Methanoperedens Vercelli Strain 1 From A Bioreactor Enrichment Culture
Organism: Candidatus methanoperedens sp.
Method: X-RAY DIFFRACTION Resolution:0.98 Å Release Date: 2025-07-23 Classification: TRANSFERASE Ligands: K, F43, EDO, TP7, COM, SHT |
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Krypton-Pressurized Methyl-Coenzyme M Reductase Of An Anme-2C Isolated From A Microbial Enrichment
Organism: Candidatus methanogasteraceae archaeon
Method: X-RAY DIFFRACTION Resolution:1.80 Å Release Date: 2025-07-16 Classification: TRANSFERASE Ligands: KR, MG, PGE, EDO, CL, TP7, F43, PEG, GOL, COM, NA, K |
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Methyl-Coenzyme M Reductase Of Anme-2D Candidatus Methanoperedens Sp. Blz2 From A Bioreactor Enrichment Culture
Organism: Candidatus methanoperedens sp. blz2
Method: X-RAY DIFFRACTION Resolution:0.98 Å Release Date: 2025-07-16 Classification: TRANSFERASE |
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Organism: Candidatus methanogasteraceae archaeon
Method: X-RAY DIFFRACTION Resolution:1.34 Å Release Date: 2025-07-16 Classification: TRANSFERASE Ligands: K, NA, CL, F43, COM, TP7, GOL, MPD, EDO |
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Crystal Structure Of The Tungsten-Dependent Aldehyde:Ferredoxin Oxidoreductase From Clostridium Autoethanogenum.
Organism: Clostridium autoethanogenum dsm 10061
Method: X-RAY DIFFRACTION Resolution:1.59 Å Release Date: 2025-05-28 Classification: OXIDOREDUCTASE Ligands: SF4, A1IJH, CL, MG, EDO |
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Structure Of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) In Complex With Acetyl-Coenyzme A From Clostridium Autoethanogenum
Organism: Clostridium autoethanogenum dsm 10061
Method: X-RAY DIFFRACTION Resolution:2.93 Å Release Date: 2025-02-12 Classification: OXIDOREDUCTASE Ligands: SF4, NI, EDO, PE4, GOL, PEG, CA, CL, XCC, ACO, TRS |
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Structure Of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) In Complex With Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3A)
Organism: Clostridium autoethanogenum dsm 10061
Method: ELECTRON MICROSCOPY Resolution:2.71 Å Release Date: 2025-02-05 Classification: OXIDOREDUCTASE Ligands: SF4, B12, NI, RQM |
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Structure Of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) In Complex With Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3B)
Organism: Clostridium autoethanogenum dsm 10061
Method: ELECTRON MICROSCOPY Resolution:2.65 Å Release Date: 2025-02-05 Classification: OXIDOREDUCTASE Ligands: SF4, NI, RQM, B12 |
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Structure Of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) In Complex With Corrinoid Iron-Sulfur Protein (Cofesp) From Clostridium Autoethanogenum (Composite Structure, Class 3Cb)
Organism: Clostridium autoethanogenum dsm 10061
Method: ELECTRON MICROSCOPY Resolution:2.88 Å Release Date: 2025-02-05 Classification: OXIDOREDUCTASE Ligands: SF4, NI, B12, RQM |
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Structure Of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) From Clostridium Autoethanogenum (Composite Structure, Closed And Co-Bound State)
Organism: Clostridium autoethanogenum dsm 10061
Method: ELECTRON MICROSCOPY Resolution:2.83 Å Release Date: 2025-02-05 Classification: OXIDOREDUCTASE Ligands: SF4, RQM, NI, CMO |
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Structure Of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) From Clostridium Autoethanogenum (Composite Structure, Semi-Extended State)
Organism: Clostridium autoethanogenum dsm 10061
Method: ELECTRON MICROSCOPY Resolution:3.29 Å Release Date: 2025-02-05 Classification: OXIDOREDUCTASE Ligands: SF4, NI, RQM |
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Structure Of Carbon Monoxide Dehydrogenase/Acetyl-Coa Synthase (Codh/Acs) In Complex With Ferredoxin (Clostridium Autoethanogenum)
Organism: Clostridium autoethanogenum dsm 10061
Method: ELECTRON MICROSCOPY Resolution:2.10 Å Release Date: 2025-02-05 Classification: OXIDOREDUCTASE Ligands: SF4, RQM |




















