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Yorodumi- EMDB-54053: Cryo-EM structure of alphaM I-domain:C3d-anti-CR3-Nb complex focu... -
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Basic information
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| Title | Cryo-EM structure of alphaM I-domain:C3d-anti-CR3-Nb complex focused refinement from the alphaM/beta2:C3d-anti-CR3-Nb headpiece complex | |||||||||
Map data | Focus map | |||||||||
Sample |
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Keywords | phagocytosis / integrin / opsonisation / IMMUNE SYSTEM | |||||||||
| Function / homology | Function and homology informationectodermal cell differentiation / integrin alphaM-beta2 complex / positive regulation of neutrophil degranulation / response to Gram-positive bacterium / response to curcumin / positive regulation of microglial cell mediated cytotoxicity / vertebrate eye-specific patterning / complement component C3b binding / complement-mediated synapse pruning / Toll Like Receptor 4 (TLR4) Cascade ...ectodermal cell differentiation / integrin alphaM-beta2 complex / positive regulation of neutrophil degranulation / response to Gram-positive bacterium / response to curcumin / positive regulation of microglial cell mediated cytotoxicity / vertebrate eye-specific patterning / complement component C3b binding / complement-mediated synapse pruning / Toll Like Receptor 4 (TLR4) Cascade / : / complement receptor mediated signaling pathway / integrin complex / heterotypic cell-cell adhesion / cargo receptor activity / phagocytosis, engulfment / negative regulation of dopamine metabolic process / forebrain development / amyloid-beta clearance / tertiary granule membrane / plasma membrane raft / positive regulation of protein targeting to membrane / Integrin cell surface interactions / response to mechanical stimulus / specific granule membrane / positive regulation of superoxide anion generation / heat shock protein binding / receptor-mediated endocytosis / response to ischemia / cell-matrix adhesion / Cell surface interactions at the vascular wall / response to amphetamine / integrin-mediated signaling pathway / microglial cell activation / cell-cell adhesion / integrin binding / response to estradiol / amyloid-beta binding / signaling receptor activity / Interleukin-4 and Interleukin-13 signaling / cell adhesion / external side of plasma membrane / innate immune response / Neutrophil degranulation / cell surface / : / extracellular exosome / metal ion binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.94 Å | |||||||||
Authors | Fruergaard MU / Andersen GR | |||||||||
| Funding support | 1 items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of alphaM I-domain:C3d-anti-CR3-Nb complex focused refinement from the alphaM/beta2:C3d-anti-CR3-Nb headpiece complex Authors: Fruergaard MU / Andersen GR | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_54053.map.gz | 32.3 MB | EMDB map data format | |
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| Header (meta data) | emd-54053-v30.xml emd-54053.xml | 24 KB 24 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_54053_fsc.xml | 8.4 KB | Display | FSC data file |
| Images | emd_54053.png | 72.4 KB | ||
| Masks | emd_54053_msk_1.map | 64 MB | Mask map | |
| Filedesc metadata | emd-54053.cif.gz | 7.1 KB | ||
| Others | emd_54053_half_map_1.map.gz emd_54053_half_map_2.map.gz | 59.4 MB 59.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-54053 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-54053 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9rmaMC ![]() 52188 ![]() 52189 ![]() 52190 ![]() 52191 ![]() 54052 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_54053.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Focus map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.29 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_54053_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: half map A
| File | emd_54053_half_map_1.map | ||||||||||||
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| Annotation | half map A | ||||||||||||
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| Density Histograms |
-Half map: half map B
| File | emd_54053_half_map_2.map | ||||||||||||
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| Annotation | half map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : alphaM I-domain:C3d-anti-CR3-Nb complex
| Entire | Name: alphaM I-domain:C3d-anti-CR3-Nb complex |
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| Components |
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-Supramolecule #1: alphaM I-domain:C3d-anti-CR3-Nb complex
| Supramolecule | Name: alphaM I-domain:C3d-anti-CR3-Nb complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 Details: alphaM I-domain:C3d-anti-CR3-Nb complex focused refinement from the alphaM/beta2:C3d-anti-CR3-Nb headpiece complex |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 190 kDa/nm |
-Macromolecule #1: Isoform 2 of Integrin alpha-M
| Macromolecule | Name: Isoform 2 of Integrin alpha-M / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 83.989734 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: FNLDTENAMT FQENARGFGQ SVVQLQGSRV VVGAPQEIVA ANQRGSLYQC DYSTGSCEPI RLQVPVEAVN MSLGLSLAAT TSPPQLLAC GPTVHQTCSE NTYVKGLCFL FGSNLRQQPQ KFPEALRGCP QEDSDIAFLI DGSGSIIPHD FRRMKEFVST V MEQLKKSK ...String: FNLDTENAMT FQENARGFGQ SVVQLQGSRV VVGAPQEIVA ANQRGSLYQC DYSTGSCEPI RLQVPVEAVN MSLGLSLAAT TSPPQLLAC GPTVHQTCSE NTYVKGLCFL FGSNLRQQPQ KFPEALRGCP QEDSDIAFLI DGSGSIIPHD FRRMKEFVST V MEQLKKSK TLFSLMQYSE EFRIHFTFKE FQNNPNPRSL VKPITQLLGR THTATGIRKV VRELFNITNG ARKNAFKILV VI TDGEKFG DPLGYEDVIP EADREGVIRY VIGVGDAFRS EKSRQELNTI ASKPPRDHVF QVNNFEALKT IQNQLREKIF AIE GTQTGS SSSFEHEMSQ EGFSAAITSN GPLLSTVGSY DWAGGVFLYT SKEKSTFINM TRVDSDMNDA YLGYAAAIIL RNRV QSLVL GAPRYQHIGL VAMFRQNTGM WESNANVKGT QIGAYFGASL CSVDVDSNGS TDLVLIGAPH YYEQTRGGQV SVCPL PRGQ RARWQCDAVL YGEQGQPWGR FGAALTVLGD VNGDKLTDVA IGAPGEEDNR GAVYLFHGTS GSGISPSHSQ RIAGSK LSP RLQYFGQSLS GGQDLTMDGL VDLTVGAQGH VLLLRSQPVL RVKAIMEFNP REVARNVFEC NDQVVKGKEA GEVRVCL HV QKSTRDRLRE GQIQSVVTYD LALDSGRPHS RAVFNETKNS TRRQTQVLGL TQTCETLKLQ LPNCIEDPVS PIVLRLNF S LVGTPLSAFG NLRPVLAEDA QRLFTALFPF EKNTGGENLY FQ UniProtKB: Integrin alpha-M |
-Macromolecule #2: C3d-anti-CR3-Nb fusion ligand
| Macromolecule | Name: C3d-anti-CR3-Nb fusion ligand / type: protein_or_peptide / ID: 2 / Details: Fused with a flexible linker to C3d / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 51.073422 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MGWSCIILFL VATATGVHQV QLVESGGGLV QAGGSLRLSC TTSGFTFDDY AIGWFRQAPG KEREGVSCIS SSEGKYYSDG GGGSGGGGS GGGGSVDAER LKHLIVTPSG SGEQNMIGMT PTVIAVHYLD ETEQWEKFGL EKRQGALELI KKGYTQQLAF R QPSSAFAA ...String: MGWSCIILFL VATATGVHQV QLVESGGGLV QAGGSLRLSC TTSGFTFDDY AIGWFRQAPG KEREGVSCIS SSEGKYYSDG GGGSGGGGS GGGGSVDAER LKHLIVTPSG SGEQNMIGMT PTVIAVHYLD ETEQWEKFGL EKRQGALELI KKGYTQQLAF R QPSSAFAA FVKRAPSTWL TAYVVKVFSL AVNLIAIDSQ VLCGAVKWLI LEKQKPDGVF QEDAPVIHQE MIGGLRNNNE KD MALTAFV LISLQEAKDI CEEQVNSLPG SITKAGDFLE ANYMNLQRSY TVAIAGYALA QMGRLKGPLL NKFLTTAKDK NRW EDPGKQ LYNVEATSYA LLALLQLKDF DFVPPVVRWL NEQRYYGGGY GSTQATFMVF QALAQYQKDA PDHKGGGGSG RFTI SSDNA KNTVYLQMNN LKPEDTAVYY CAAEWNNFGR LCMYPDYWGQ GTQVTVSSEN LYFQGHHHHH H |
-Macromolecule #4: MANGANESE (II) ION
| Macromolecule | Name: MANGANESE (II) ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: MN |
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| Molecular weight | Theoretical: 54.938 Da |
-Macromolecule #5: water
| Macromolecule | Name: water / type: ligand / ID: 5 / Number of copies: 2 / 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
| Concentration | 2.88 mg/mL | |||||||||||||||
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| Buffer | pH: 7.5 Component:
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| Grid | Model: UltrAuFoil R0./1 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 180 sec. / Details: 25 mA current | |||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV Details: 0.02 % w/v CHAPS added to sample just before vitrification. |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.1 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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| Output model | ![]() PDB-9rma: |
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Keywords
Homo sapiens (human)
Authors
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FIELD EMISSION GUN

