+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-41101 | |||||||||
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Title | 33-mer FliF MS-ring from Salmonella | |||||||||
Map data | ||||||||||
Sample |
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Keywords | MS-ring / Symmetry mismatch / Flagellar component / Membrane protein / MOTOR PROTEIN | |||||||||
Function / homology | Function and homology information bacterial-type flagellum basal body, MS ring / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / plasma membrane Similarity search - Function | |||||||||
Biological species | Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Singh PK / Iverson TM | |||||||||
Funding support | United States, 1 items
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Citation | Journal: To Be Published Title: Structural basis for directional rotation of the Salmonella flagellum Authors: Singh PK / Iverson TM | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_41101.map.gz | 869.3 MB | EMDB map data format | |
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Header (meta data) | emd-41101-v30.xml emd-41101.xml | 14.9 KB 14.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_41101_fsc.xml | 29.6 KB | Display | FSC data file |
Images | emd_41101.png | 152.9 KB | ||
Masks | emd_41101_msk_1.map | 1.7 GB | Mask map | |
Filedesc metadata | emd-41101.cif.gz | 5.4 KB | ||
Others | emd_41101_half_map_1.map.gz emd_41101_half_map_2.map.gz | 1.6 GB 1.6 GB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-41101 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-41101 | HTTPS FTP |
-Validation report
Summary document | emd_41101_validation.pdf.gz | 994.6 KB | Display | EMDB validaton report |
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Full document | emd_41101_full_validation.pdf.gz | 994.1 KB | Display | |
Data in XML | emd_41101_validation.xml.gz | 34.5 KB | Display | |
Data in CIF | emd_41101_validation.cif.gz | 47.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-41101 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-41101 | HTTPS FTP |
-Related structure data
Related structure data | 8t8pMC 8t8oC C: citing same article (ref.) M: atomic model generated by this map |
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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_41101.map.gz / Format: CCP4 / Size: 1.7 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.363 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_41101_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_41101_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_41101_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM,...
Entire | Name: Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM, and FliN |
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Components |
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-Supramolecule #1: Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM,...
Supramolecule | Name: Flagellar MS-ring and C-ring complex containing FliF, FliG, FliM, and FliN type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) |
Molecular weight | Theoretical: 2 MDa |
-Macromolecule #1: Flagellar M-ring protein
Macromolecule | Name: Flagellar M-ring protein / type: protein_or_peptide / ID: 1 / Number of copies: 33 / Enantiomer: LEVO |
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Source (natural) | Organism: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) |
Molecular weight | Theoretical: 61.295645 KDa |
Recombinant expression | Organism: Escherichia coli BL21(DE3) (bacteria) |
Sequence | String: MSATASTATQ PKPLEWLNRL RANPRIPLIV AGSAAVAIVV AMVLWAKTPD YRTLFSNLSD QDGGAIVAQL TQMNIPYRFA NGSGAIEVP ADKVHELRLR LAQQGLPKGG AVGFELLDQE KFGISQFSEQ VNYQRALEGE LARTIETLGP VKSARVHLAM P KPSLFVRE ...String: MSATASTATQ PKPLEWLNRL RANPRIPLIV AGSAAVAIVV AMVLWAKTPD YRTLFSNLSD QDGGAIVAQL TQMNIPYRFA NGSGAIEVP ADKVHELRLR LAQQGLPKGG AVGFELLDQE KFGISQFSEQ VNYQRALEGE LARTIETLGP VKSARVHLAM P KPSLFVRE QKSPSASVTV TLEPGRALDE GQISAVVHLV SSAVAGLPPG NVTLVDQSGH LLTQSNTSGR DLNDAQLKFA ND VESRIQR RIEAILSPIV GNGNVHAQVT AQLDFANKEQ TEEHYSPNGD ASKATLRSRQ LNISEQVGAG YPGGVPGALS NQP APPNEA PIATPPTNQQ NAQNTPQTST STNSNSAGPR STQRNETSNY EVDRTIRHTK MNVGDIERLS VAVVVNYKTL ADGK PLPLT ADQMKQIEDL TREAMGFSDK RGDTLNVVNS PFSAVDNTGG ELPFWQQQSF IDQLLAAGRW LLVLVVAWIL WRKAV RPQL TRRVEEAKAA QEQAQVRQET EEAVEVRLSK DEQLQQRRAN QRLGAEVMSQ RIREMSDNDP RVVALVIRQW MSNDHE UniProtKB: Flagellar M-ring protein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 51.557 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: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |