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- EMDB-37754: Fe-O nanocluster of form-IX in the 4-fold channel of Ureaplasma d... -
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Open data
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Basic information
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Title | Fe-O nanocluster of form-IX in the 4-fold channel of Ureaplasma diversum ferritin | |||||||||
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![]() | ferritin / METAL BINDING PROTEIN | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
![]() | Wang WM / Ma DY / Gong WJ / Wu LJ / Wang HF | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Growth Process of Fe-O Nanoclusters with Different Sizes Biosynthesized by Protein Nanocages. Authors: Wenming Wang / Hongfang Xi / Dan Fu / Danyang Ma / Wenjun Gong / Yaqin Zhao / Xiaomei Li / Lijie Wu / Yu Guo / Guanghua Zhao / Hongfei Wang / ![]() Abstract: All protein-directed syntheses of metal nanoclusters (NCs) and nanoparticles (NPs) have attracted considerable attention because protein scaffolds provide a unique metal coordination environment and ...All protein-directed syntheses of metal nanoclusters (NCs) and nanoparticles (NPs) have attracted considerable attention because protein scaffolds provide a unique metal coordination environment and can adjust the shape and morphology of NCs and NPs. However, the detailed formation mechanisms of NCs or NPs directed by protein templates remain unclear. In this study, by taking advantage of the ferritin nanocage as a biotemplate to monitor the growth of Fe-O NCs as a function of time, we synthesized a series of iron NCs with different sizes and shapes and subsequently solved their corresponding three-dimensional atomic-scale structures by X-ray protein crystallography and cryo-electron microscopy. The time-dependent structure analyses revealed the growth process of these Fe-O NCs with the 4-fold channel of ferritin as nucleation sites. To our knowledge, the newly biosynthesized FeOGlu represents the largest Fe-O NCs with a definite atomic structure. This study contributes to our understanding of the formation mechanism of iron NCs and provides an effective method for metal NC synthesis. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14 KB 14 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.7 KB | Display | ![]() |
Images | ![]() | 172.7 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Others | ![]() ![]() | 59 MB 59 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 957.5 KB | Display | ![]() |
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Full document | ![]() | 957 KB | Display | |
Data in XML | ![]() | 16.2 KB | Display | |
Data in CIF | ![]() | 21.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8wquMC ![]() 8w6mC ![]() 8w6qC ![]() 8w6sC ![]() 8w6uC ![]() 8w6yC ![]() 8w73C ![]() 8w74C ![]() 8w79C ![]() 8w7bC ![]() 8w7oC ![]() 8w7qC ![]() 8w7tC ![]() 8w7uC ![]() 8w7vC ![]() 8wptC ![]() 8wpvC ![]() 8wqvC ![]() 8wqxC ![]() 8wqyC ![]() 8wr0C M: atomic model generated by this map C: citing same article ( |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0469 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_37754_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_37754_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : ferritin
Entire | Name: ferritin |
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Components |
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-Supramolecule #1: ferritin
Supramolecule | Name: ferritin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: ferritin
Macromolecule | Name: ferritin / type: protein_or_peptide / ID: 1 / Details: WP_081847832.1 / Number of copies: 24 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 21.254996 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLYRERNNIM QKSNKINDAL NQHYKLNVEL GLVYAHYAHV ADDEFDMPYL GKFIQHLSED KLGVHKEYIS DYFKRNGMKL KTDVSVAVK SIPSDAKALI QEVYARENEV RDHVKAIAKL ALAEDDYESF YFIQWYVRDG LKDLTEVDDV VKLFNSSNDK L IIEETIKE MVEKEESEHE IWG |
-Macromolecule #2: FE (III) ION
Macromolecule | Name: FE (III) ION / type: ligand / ID: 2 / Number of copies: 24 / Formula: FE |
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Molecular weight | Theoretical: 55.845 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 2 mg/mL |
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Buffer | pH: 8 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy
Microscope | FEI TECNAI F30 |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DARK FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |