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Open data
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Basic information
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| Title | Demo apoferritin data for Magellon | |||||||||
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Sample |
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Keywords | METAL BINDING PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.7 Å | |||||||||
Authors | Stagg SM / Khoshbin B / Damodar P / Cianfrocco MA / Lander GC | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: IUCrJ / Year: 2025Title: Magellon - an extensible platform for cryo-EM data visualization, management and processing. Authors: Behdad Khoshbin / Puneeth Damodar / Rupali R Garje / Frank H Schotanus / Nandagopal Nair / Lai Wei / Jan Hannes Schäfer / Gabriel C Lander / Michael A Cianfrocco / Scott M Stagg / ![]() Abstract: Single-particle cryo-electron microscopy (cryo-EM) has revolutionized structural biology by enabling high-resolution determination of macromolecular structures. However, the field faces challenges in ...Single-particle cryo-electron microscopy (cryo-EM) has revolutionized structural biology by enabling high-resolution determination of macromolecular structures. However, the field faces challenges in data management, processing workflow integration and software extensibility. We present Magellon, an innovative cryo-EM software platform that addresses these challenges through a modern microservices architecture. Magellon consists of an extensible backend with a web based frontend that we call Magellon Viewer. Together, these combine high-performance computing capabilities with an intuitive user interface, enabling researchers to efficiently process and analyze cryo-EM data. The platform's distinguishing features include a plugin based architecture, distributed processing capabilities, comprehensive monitoring systems, and a novel approach to data organization and visualization. A key philosophy of the approach is that the Magellon backend provides a platform that uses robust industry-standard libraries to orchestrate computational tasks while offering users and developers flexibility in selecting the computational resources for performing calculations. Magellon represents a significant advancement in cryo-EM software infrastructure, offering flexibility, scalability and extensibility while maintaining ease of use. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_49574.map.gz | 59.7 MB | EMDB map data format | |
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| Header (meta data) | emd-49574-v30.xml emd-49574.xml | 14.7 KB 14.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_49574_fsc.xml | 9.1 KB | Display | FSC data file |
| Images | emd_49574.png | 102.6 KB | ||
| Filedesc metadata | emd-49574.cif.gz | 4.9 KB | ||
| Others | emd_49574_half_map_1.map.gz emd_49574_half_map_2.map.gz | 46.2 MB 46.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-49574 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-49574 | HTTPS FTP |
-Validation report
| Summary document | emd_49574_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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| Full document | emd_49574_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | emd_49574_validation.xml.gz | 16 KB | Display | |
| Data in CIF | emd_49574_validation.cif.gz | 21 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49574 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49574 | HTTPS FTP |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_49574.map.gz / Format: CCP4 / Size: 64 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: 0.78989 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_49574_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_49574_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Ferritin heavy chain, N-terminally processed
| Entire | Name: Ferritin heavy chain, N-terminally processed |
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| Components |
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-Supramolecule #1: Ferritin heavy chain, N-terminally processed
| Supramolecule | Name: Ferritin heavy chain, N-terminally processed / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Mouse apoferritin heavy chain
| Macromolecule | Name: Mouse apoferritin heavy chain / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Recombinant expression | Organism: ![]() |
| Sequence | String: PSQVRQNYHQ DAEAAINRQI NLELYASYVY LSMSCYFDRD DVALKNFAKY FLHQSHEERE HAEKLMKLQN QRGGRIFLQD IKKPDRDDW ESGLNAMECA LHLEKSVNQS LLELHKLATD KNDPHLCDFI ETYYLSEQVK SIKELGDHVT NLRKMGAPEA G MAEYLFDK HTLG |
-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: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: DIRECT ELECTRON APOLLO (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 / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
United States, 1 items
Citation
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Processing
FIELD EMISSION GUN

