|Entry||Database: EMDB / ID: EMD-4905|
|Title||3D structure of horse spleen apoferritin determined using multifunctional graphene supports for electron cryomicroscopy|
Ferritin light chain
|Function / homology|
Function and homology information
intracellular ferritin complex / autolysosome / intracellular sequestering of iron ion / ferric iron binding / ferrous iron binding / iron ion transport / oxidation-reduction process / iron ion binding / identical protein binding / cytoplasm
Ferritin / Ferritin iron-binding regions signature 1. / Ferritin, conserved site / Ferritin-like / Ferritin-like superfamily / Ferritin-like diiron domain / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin iron-binding regions signature 2. / Ferritin-like diiron domain profile.
Ferritin light chain
|Biological species||Equus caballus (horse) / Horse (horse)|
|Method||single particle reconstruction / cryo EM / Resolution: 2.1 Å|
|Authors||Naydenova K / Peet MJ / Russo CJ|
|Citation||Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2019|
Title: Multifunctional graphene supports for electron cryomicroscopy.
Authors: Katerina Naydenova / Mathew J Peet / Christopher J Russo /
Abstract: With recent technological advances, the atomic resolution structure of any purified biomolecular complex can, in principle, be determined by single-particle electron cryomicroscopy (cryoEM). In ...With recent technological advances, the atomic resolution structure of any purified biomolecular complex can, in principle, be determined by single-particle electron cryomicroscopy (cryoEM). In practice, the primary barrier to structure determination is the preparation of a frozen specimen suitable for high-resolution imaging. To address this, we present a multifunctional specimen support for cryoEM, comprising large-crystal monolayer graphene suspended across the surface of an ultrastable gold specimen support. Using a low-energy plasma surface modification system, we tune the surface of this support to the specimen by patterning a range of covalent functionalizations across the graphene layer on a single grid. This support design reduces specimen movement during imaging, improves image quality, and allows high-resolution structure determination with a minimum of material and data.
|Validation Report||PDB-ID: 6rjh|
SummaryFull reportAbout validation report
|Date||Deposition: Apr 26, 2019 / Header (metadata) release: Jun 5, 2019 / Map release: Jun 5, 2019 / Update: Jun 19, 2019|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_4905.map.gz / Format: CCP4 / Size: 149.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.6495 Å|
|Symmetry||Space group: 1|
CCP4 map header:
|Entire||Name: ApoferritinFerritin / Number of components: 2|
-Component #1: protein, Apoferritin
|Protein||Name: ApoferritinFerritin / Recombinant expression: No|
|Source||Species: Equus caballus (horse)|
-Component #2: protein, Ferritin light chain
|Protein||Name: Ferritin light chain / Number of Copies: 24 / Recombinant expression: No|
|Mass||Theoretical: 19.532113 kDa|
|Source||Species: Horse (horse)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.4|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 37 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI FALCON III (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: O (octahedral) / Number of projections: 41202|
|3D reconstruction||Software: RELION / Resolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF|
|FSC plot (resolution estimation)|
-Atomic model buiding
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