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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Nitrogenase maturase NifEN | |||||||||
Map data | ||||||||||
Sample |
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Keywords | nitrogenase cofactor maturase / METAL BINDING PROTEIN | |||||||||
| Function / homology | Function and homology informationnitrogenase activity / 4 iron, 4 sulfur cluster binding / protein-containing complex assembly / metal ion binding Similarity search - Function | |||||||||
| Biological species | Azotobacter vinelandii (bacteria) / Azotobacter vinelandii DJ (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.14 Å | |||||||||
Authors | Schneider FF / Martin del Campo JS / Zhang L / Dean DR / Einsle O | |||||||||
| Funding support | European Union, Germany, 2 items
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Citation | Journal: To Be PublishedTitle: Trafficking of a nitrogenase FeMo-cofactor assembly intermediate Authors: Schneider FF / Martin del Campo JS / Zhang L / Dean DR / Einsle O | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_52783.map.gz | 49.1 MB | EMDB map data format | |
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| Header (meta data) | emd-52783-v30.xml emd-52783.xml | 21.9 KB 21.9 KB | Display Display | EMDB header |
| Images | emd_52783.png | 115.5 KB | ||
| Masks | emd_52783_msk_1.map | 52.7 MB | Mask map | |
| Filedesc metadata | emd-52783.cif.gz | 6.4 KB | ||
| Others | emd_52783_additional_1.map.gz emd_52783_half_map_1.map.gz emd_52783_half_map_2.map.gz | 49.2 MB 49 MB 49 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-52783 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-52783 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9iaoMC ![]() 9ianC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_52783.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.7627 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_52783_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: #1
| File | emd_52783_additional_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_52783_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_52783_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Hetero-hexameric complex of NifEN and NifX
| Entire | Name: Hetero-hexameric complex of NifEN and NifX |
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| Components |
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-Supramolecule #1: Hetero-hexameric complex of NifEN and NifX
| Supramolecule | Name: Hetero-hexameric complex of NifEN and NifX / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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| Source (natural) | Organism: Azotobacter vinelandii (bacteria) |
-Macromolecule #1: Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE
| Macromolecule | Name: Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Azotobacter vinelandii DJ (bacteria) |
| Molecular weight | Theoretical: 51.948211 KDa |
| Recombinant expression | Organism: Azotobacter vinelandii DJ (bacteria) |
| Sequence | String: MKAKDIAELL DEPACSHNKK EKSGCAKPKP GATDGGCSFD GAQIALLPVA DVAHIVHGPI ACAGSSWDNR GTRSSGPDLY RIGMTTDLT ENDVIMGRAE KRLFHAIRQA VESYSPPAVF VYNTCVPALI GDDVDAVCKA AAERFGTPVI PVDSAGFYGT K NLGNRIAG ...String: MKAKDIAELL DEPACSHNKK EKSGCAKPKP GATDGGCSFD GAQIALLPVA DVAHIVHGPI ACAGSSWDNR GTRSSGPDLY RIGMTTDLT ENDVIMGRAE KRLFHAIRQA VESYSPPAVF VYNTCVPALI GDDVDAVCKA AAERFGTPVI PVDSAGFYGT K NLGNRIAG EAMLKYVIGT REPDPLPVGS ERPGIRVHDV NLIGEYNIAG EFWHVLPLLD ELGLRVLCTL AGDARYREVQ TM HRAEVNM MVCSKAMLNV ARKLQETYGT PWFEGSFYGI TDTSQALRDF ARLLDDPDLT ARTEALIARE EAKVRAALEP WRA RLEGKR VLLYTGGVKS WSVVSALQDL GMKVVATGTK KSTEEDKARI RELMGDDVKM LDEGNARVLL KTVDEYQADI LIAG GRNMY TALKGRVPFL DINQEREFGY AGYDGMLELV RQLCITLECP VWEAVRRPAP WDIPASQDAA PSAPARSANA UniProtKB: Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE |
-Macromolecule #2: Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN
| Macromolecule | Name: Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Azotobacter vinelandii DJ (bacteria) |
| Molecular weight | Theoretical: 49.301969 KDa |
| Recombinant expression | Organism: Azotobacter vinelandii DJ (bacteria) |
| Sequence | String: MAEIINRNKA LAVSPLKASQ TMGAALAILG LARSMPLFHG SQGCTAFAKV FFVRHFREPV PLQTTAMDQV SSVMGADENV VEALKTICE RQNPSVIGLL TTGLSETQGC DLHTALHEFR TQYEEYKDVP IVPVNTPDFS GCFESGFAAA VKAIVETLVP E RRDQVGKR ...String: MAEIINRNKA LAVSPLKASQ TMGAALAILG LARSMPLFHG SQGCTAFAKV FFVRHFREPV PLQTTAMDQV SSVMGADENV VEALKTICE RQNPSVIGLL TTGLSETQGC DLHTALHEFR TQYEEYKDVP IVPVNTPDFS GCFESGFAAA VKAIVETLVP E RRDQVGKR PRQVNVLCSA NLTPGDLEYI AESIESFGLR PLLIPDLSGS LDGHLDENRF NALTTGGLSV AELATAGQSV AT LVVGQSL AGAADALAER TGVPDRRFGM LYGLDAVDAW LMALAEISGN PVPDRYKRQR AQLQDAMLDT HFMLSSARTA IAA DPDLLL GFDALLRSMG AHTVAAVVPA RAAALVDSPL PSVRVGDLED LEHAARAGQA QLVIGNSHAL ASARRLGVPL LRAG FPQYD LLGGFQRCWS GYRGSSQVLF DLANLLVEHH QGIQPYHSIY AQKPATEQPQ WRH UniProtKB: Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN |
-Macromolecule #3: Nitrogenase MoFe cofactor biosynthesis protein NifX
| Macromolecule | Name: Nitrogenase MoFe cofactor biosynthesis protein NifX / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Azotobacter vinelandii DJ (bacteria) |
| Molecular weight | Theoretical: 17.30751 KDa |
| Recombinant expression | Organism: Azotobacter vinelandii DJ (bacteria) |
| Sequence | String: MSSPTRQLQV LDSEDDGTLL KVAFASSDRE LVDQHFGSSR SFAIYGVNPE RSQLLSVVEF GELEQDGNED KLARKIDLLD GCVAVYCCA CGASAVRQLM AIGVQPIKVS EGARIAELIE ALQVELREGP SAWLAKAIQR TRGPDMRRFD AMAAEGWDE UniProtKB: Nitrogenase MoFe cofactor biosynthesis protein NifX |
-Macromolecule #4: FeFe cofactor
| Macromolecule | Name: FeFe cofactor / type: ligand / ID: 4 / Number of copies: 2 / Formula: S5Q |
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| Molecular weight | Theoretical: 747.356 Da |
| Chemical component information | ![]() ChemComp-S5Q: |
-Macromolecule #5: IRON/SULFUR CLUSTER
| Macromolecule | Name: IRON/SULFUR CLUSTER / type: ligand / ID: 5 / Number of copies: 2 / Formula: SF4 |
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| Molecular weight | Theoretical: 351.64 Da |
| Chemical component information | ![]() ChemComp-FS1: |
-Macromolecule #6: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 2 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #7: water
| Macromolecule | Name: water / type: ligand / ID: 7 / Number of copies: 883 / Formula: HOH |
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| Molecular weight | Theoretical: 18.015 Da |
| Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Azotobacter vinelandii (bacteria)
Authors
Germany, 2 items
Citation



Z (Sec.)
Y (Row.)
X (Col.)























































Processing
FIELD EMISSION GUN
