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- PDB-6s61: Apoferritin from mouse at 1.84 angstrom resolution -

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Basic information

Entry
Database: PDB / ID: 6s61
TitleApoferritin from mouse at 1.84 angstrom resolution
ComponentsFerritin heavy chain
KeywordsMETAL BINDING PROTEIN / iron ion binding / ferroxidase / iron storage / cytoplasm
Function / homology
Function and homology information


Golgi Associated Vesicle Biogenesis / Neutrophil degranulation / Iron uptake and transport / autolysosome / ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / negative regulation of fibroblast proliferation / endocytic vesicle lumen / ferric iron binding ...Golgi Associated Vesicle Biogenesis / Neutrophil degranulation / Iron uptake and transport / autolysosome / ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / negative regulation of fibroblast proliferation / endocytic vesicle lumen / ferric iron binding / ferrous iron binding / iron ion transport / immune response / iron ion binding / negative regulation of cell population proliferation / mitochondrion / extracellular region / identical protein binding / cytoplasm
Ferritin/DPS protein domain / Ferritin iron-binding regions signature 2. / Ferritin / Ferritin-like superfamily / Ferritin-like / Ferritin, conserved site / Ferritin-like diiron domain / Ferritin-like domain / Ferritin iron-binding regions signature 1. / Ferritin-like diiron domain profile.
Ferritin heavy chain
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 1.84 Å
AuthorsVonck, J. / Pfeil-Gardiner, O. / Mills, D.J.
CitationJournal: To Be Published
Title: To be published later
Authors: Vonck, J. / Mills, D.J. / Pfeil-Gardiner, O.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Jul 2, 2019 / Release: Jul 10, 2019
RevisionDateData content typeProviderType
1.0Jul 10, 2019Structure modelrepositoryInitial release

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Structure visualization

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Assembly

Deposited unit
A: Ferritin heavy chain
B: Ferritin heavy chain
C: Ferritin heavy chain
D: Ferritin heavy chain
E: Ferritin heavy chain
F: Ferritin heavy chain
G: Ferritin heavy chain
H: Ferritin heavy chain
I: Ferritin heavy chain
J: Ferritin heavy chain
K: Ferritin heavy chain
L: Ferritin heavy chain
M: Ferritin heavy chain
N: Ferritin heavy chain
O: Ferritin heavy chain
P: Ferritin heavy chain
Q: Ferritin heavy chain
R: Ferritin heavy chain
S: Ferritin heavy chain
T: Ferritin heavy chain
U: Ferritin heavy chain
V: Ferritin heavy chain
W: Ferritin heavy chain
X: Ferritin heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)508,24854
Polymers506,34324
Non-polymers1,90530
Water69,4303854
1


TypeNameSymmetry operationNumber
identity operation1_5551
Buried area95410 Å2
ΔGint-1412 kcal/mol
Surface area142940 Å2
MethodPISA

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Components

#1: Protein/peptide ...
Ferritin heavy chain / / Ferritin H subunit


Mass: 21097.631 Da / Num. of mol.: 24
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Fth1, Fth / Production host: Escherichia coli (E. coli) / References: UniProt: P09528, ferroxidase
#2: Chemical
ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Fe / Iron
#3: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Formula: Zn / Zinc
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 3854 / Source method: isolated from a natural source / Formula: H2O / Water
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Octahedral complex of 24 apoferritin chains / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT
Molecular weightValue: 0.5 MDa / Experimental value: NO
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
Buffer component

Buffer-ID: 1

IDConc.NameFormula
15 mMHEPES
275 mMNaClSodium chloride
SpecimenConc.: 1.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 283 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 120000 X / Calibrated magnification: 182927 X / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm / Calibrated defocus min: 200 nm / Calibrated defocus max: 2000 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 30 sec. / Electron dose: 30 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 1788
Details: Some images were discarding after motion correction (MotionCor2) and ctf estimation (CTFfind4), leaving 1745 for processing.

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Processing

SoftwareName: PHENIX / Version: 1.12_2829: / Classification: refinement
EM software
IDNameVersionCategory
1SPHIREparticle selection
2EPUimage acquisition
4CTFFIND4CTF correction
7Coot0.8.9.1model fitting
9PHENIXmodel refinement
12RELION3classification
13RELION33D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 477115
SymmetryPoint symmetry: O (octahedral)
3D reconstructionResolution: 1.84 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 441902 / Symmetry type: POINT
Atomic model buildingProtocol: OTHER / Space: REAL / Details: phenix.real-space-refine
Atomic model buildingPDB-ID: 2CIH

2cih

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