+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-32053 | |||||||||
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Title | Macroglobulin family protein | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.1 Å | |||||||||
Authors | Huang X / Wang Y | |||||||||
Funding support | China, 1 items
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Citation | Journal: Sci China Life Sci / Year: 2022 Title: Cryo-EM structures reveal the dynamic transformation of human alpha-2-macroglobulin working as a protease inhibitor. Authors: Xiaoxing Huang / Youwang Wang / Cong Yu / Hui Zhang / Qiang Ru / Xinxin Li / Kai Song / Min Zhou / Ping Zhu / Abstract: Human alpha-2-macroglobulin is a well-known inhibitor of a broad spectrum of proteases and plays important roles in immunity, inflammation, and infections. Here, we report the cryo-EM structures of ...Human alpha-2-macroglobulin is a well-known inhibitor of a broad spectrum of proteases and plays important roles in immunity, inflammation, and infections. Here, we report the cryo-EM structures of human alpha-2-macroglobulin in its native state, induced state transformed by its authentic substrate, human trypsin, and serial intermediate states between the native and fully induced states. These structures exhibit distinct conformations, which reveal the dynamic transformation of alpha-2-macro-globulin that acts as a protease inhibitor. The results shed light on the molecular mechanism of alpha-2-macroglobulin in entrapping substrates. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_32053.map.gz | 95.5 MB | EMDB map data format | |
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Header (meta data) | emd-32053-v30.xml emd-32053.xml | 7.4 KB 7.4 KB | Display Display | EMDB header |
Images | emd_32053.png | 89.3 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32053 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32053 | HTTPS FTP |
-Validation report
Summary document | emd_32053_validation.pdf.gz | 518.2 KB | Display | EMDB validaton report |
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Full document | emd_32053_full_validation.pdf.gz | 517.8 KB | Display | |
Data in XML | emd_32053_validation.xml.gz | 6.3 KB | Display | |
Data in CIF | emd_32053_validation.cif.gz | 7.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32053 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32053 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_32053.map.gz / Format: CCP4 / Size: 103 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: 1.04 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : macroglobulin family protein
Entire | Name: macroglobulin family protein |
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Components |
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-Supramolecule #1: macroglobulin family protein
Supramolecule | Name: macroglobulin family protein / type: tissue / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | tissue |
-Sample preparation
Buffer | pH: 7.2 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 78550 |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |