+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-26377 | |||||||||
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Title | Glutamine Synthetase Type III from Ostreococcus tauri | |||||||||
Map data | ||||||||||
Sample |
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Keywords | hexamer / glutamine / LIGASE | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Ostreococcus tauri (plant) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Novikova IV / Powell SM / Evans JE | |||||||||
Funding support | United States, 2 items
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Citation | Journal: To Be Published Title: Eukaryotic Glutamine Synthetase Type III Assembles as a Hexamer and Lacks Ring-Ring Quaternary Contacts. Authors: Novikova IV / Powell SM / Smallwood CR / Purvine SO / Zhou M / Evans JE | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_26377.map.gz | 15.2 MB | EMDB map data format | |
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Header (meta data) | emd-26377-v30.xml emd-26377.xml | 13.3 KB 13.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_26377_fsc.xml | 7.5 KB | Display | FSC data file |
Images | emd_26377.png | 116.1 KB | ||
Filedesc metadata | emd-26377.cif.gz | 5.3 KB | ||
Others | emd_26377_half_map_1.map.gz emd_26377_half_map_2.map.gz | 28.3 MB 28.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-26377 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26377 | HTTPS FTP |
-Validation report
Summary document | emd_26377_validation.pdf.gz | 804.5 KB | Display | EMDB validaton report |
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Full document | emd_26377_full_validation.pdf.gz | 804 KB | Display | |
Data in XML | emd_26377_validation.xml.gz | 14.1 KB | Display | |
Data in CIF | emd_26377_validation.cif.gz | 18.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26377 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26377 | HTTPS FTP |
-Related structure data
Related structure data | 7u6oMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_26377.map.gz / Format: CCP4 / Size: 30.5 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: 1.3018 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_26377_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_26377_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : A hexamer complex of eukaryotic glutamine synthetase type III
Entire | Name: A hexamer complex of eukaryotic glutamine synthetase type III |
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Components |
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-Supramolecule #1: A hexamer complex of eukaryotic glutamine synthetase type III
Supramolecule | Name: A hexamer complex of eukaryotic glutamine synthetase type III type: cell / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Ostreococcus tauri (plant) |
-Macromolecule #1: Glutamine synthetase
Macromolecule | Name: Glutamine synthetase / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: glutamine synthetase |
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Source (natural) | Organism: Ostreococcus tauri (plant) |
Molecular weight | Theoretical: 80.09807 KDa |
Recombinant expression | Organism: Triticum aestivum (bread wheat) |
Sequence | String: MDYKDHDGDY KDHDIDYKDD DDKLALSMSS GPATTEGFGS ACFKGAVADK YLSKYGESST LLANGKWTKD MAKADIVAKA VLDWAVENG ASVYCHWFQP MGSSGVRHGN SGQVHQSMFN FAEDGTPYYS FTGEQLLQGE TDGSSFPNGG MRATHTAGGY L SIDPYSPI ...String: MDYKDHDGDY KDHDIDYKDD DDKLALSMSS GPATTEGFGS ACFKGAVADK YLSKYGESST LLANGKWTKD MAKADIVAKA VLDWAVENG ASVYCHWFQP MGSSGVRHGN SGQVHQSMFN FAEDGTPYYS FTGEQLLQGE TDGSSFPNGG MRATHTAGGY L SIDPYSPI FLREDTVFIP AAFVSYNGDA LDEKTPLHRA TDALDKQTKR MLKAMKYDVG SASVYANIGL EQEIFLTPRH AF YRRPDLQ FTGRTITGKF PARGQEMSDH YMAPISRATG AFECMRQIQQ ECFKMGIPLK TRHREVAPNQ YEFAPMFGNA ISQ VDQNLM IMQVIEEVAS EHGLAALLQE KPFAGVNGSG KHNNWSIGTS DGLNLMNPKQ VNAKTGNPEI FPLVMAAMVS AVDK HGDLM RAAIASPGND FRLGAMEAPP AVMSTYLGPS LTEFLNTVKN GSLGEYAPKK KPLEFGSDTL PSIEVPAEDR NRTSP FPYG GNRFEFRAAG SSQNVSLVNT VLNTIAAEAF KIVADRLEAG EKPLAIAQDL LKTHDKCIFN GNGYDPAWPD EAVKRG IWR IDAGCDAINE LDSAKNVTLF EGMGIFTARE IQARKSVLLG HYVGSVEMEA LTMIDMINQH VIPSVKKADL GNPSKLV DA VKTIKGAVAQ IHGTEDEHKA ATLARTLRLT TMVAIREIID EFESRCPPED WTLATYSELL FFDTYPESEY GCGGGGSH H HHHHHHHH UniProtKB: Glutamine synthetase type III N terminal-domain-containing protein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 1.2 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 100.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 5.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |