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- EMDB-4191: In situ cryo-electron tomogram from Rat neuron with C9ORF72 Poly-... -

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Entry
Database: EMDB / ID: 4191
TitleIn situ cryo-electron tomogram from Rat neuron with C9ORF72 Poly-GA aggregates
Map dataTomogram of Rat neuron cell
Samplein situ tomogram from Rat neuron:
SourceRattus norvegicus (Norway rat)
Methodelectron tomography / cryo EM
AuthorsGuo Q / Lehmer C / Martinez-Sanchez A / Rudack T / Beck F / Hartmann H / Hipp MS / Hartl FU / Edbauer D / Baumeister W / Fernandez-Busnadiego F
CitationJournal: Cell / Year: 2018
Title: In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
Authors: Qiang Guo / Carina Lehmer / Antonio Martínez-Sánchez / Till Rudack / Florian Beck / Hannelore Hartmann / Manuela Pérez-Berlanga / Frédéric Frottin / Mark S Hipp / F Ulrich Hartl / Dieter Edbauer / Wolfgang Baumeister / Rubén Fernández-Busnadiego
Abstract: Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of many neurodegenerative diseases. Here, we address the elusive link between these phenomena by employing ...Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of many neurodegenerative diseases. Here, we address the elusive link between these phenomena by employing cryo-electron tomography to dissect the molecular architecture of protein aggregates within intact neurons at high resolution. We focus on the poly-Gly-Ala (poly-GA) aggregates resulting from aberrant translation of an expanded GGGGCC repeat in C9orf72, the most common genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia. We find that poly-GA aggregates consist of densely packed twisted ribbons that recruit numerous 26S proteasome complexes, while other macromolecules are largely excluded. Proximity to poly-GA ribbons stabilizes a transient substrate-processing conformation of the 26S proteasome, suggesting stalled degradation. Thus, poly-GA aggregates may compromise neuronal proteostasis by driving the accumulation and functional impairment of a large fraction of cellular proteasomes.
DateDeposition: Dec 5, 2017 / Header (metadata) release: Jan 17, 2018 / Map release: Feb 7, 2018 / Last update: Feb 21, 2018

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Structure visualization

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  • Imaged by UCSF Chimera
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Supplemental images

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Map

Fileemd_4191.map.gz (map file in CCP4 format, 243524 KB)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
71 pix
13.68 Å/pix.
= 971.28 Å
926 pix
13.68 Å/pix.
= 12667.681 Å
926 pix
13.68 Å/pix.
= 12667.681 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 13.68 Å
Density
Minimum - Maximum-21541.451000000000931 - 6443.688500000000204
Average (Standard dev.)0.25738844 (464.516700000000014)
Details

EMDB XML:

Space Group Number1
Map Geometry
Axis orderXYZ
Dimensions92692671
Origin0.00.011.0
Limit925.0925.081.0
Spacing92692671
CellA: 12667.681 Å / B: 12667.681 Å / C: 971.28 Å
α=β=γ: 90.0 deg.

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z13.68000107991413.68000107991413.68
M x/y/z92692671
origin x/y/z0.0000.0000.000
length x/y/z12667.68112667.681971.280
α/β/γ90.00090.00090.000
start NX/NY/NZ
NX/NY/NZ
MAP C/R/S123
start NC/NR/NS0011
NC/NR/NS92692671
D min/max/mean-21541.4516443.6880.257

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Supplemental data

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Sample components

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Entire in situ tomogram from Rat neuron

EntireName: in situ tomogram from Rat neuron / Number of components: 1

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Component #1: cellular-component, in situ tomogram from Rat neuron

Cellular-componentName: in situ tomogram from Rat neuron / Recombinant expression: No
SourceSpecies: Rattus norvegicus (Norway rat)

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Experimental details

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Sample preparation

SpecimenSpecimen state: cell / Method: cryo EM
Sample solutionpH: 7
Support filmThe grid was coated with C prior to use
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: OTHER / Temperature: 298 K / Humidity: 100 %

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 1.8 e/Å2 / Illumination mode: FLOOD BEAM
LensMagnification: 42000.0 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 5000.0 - 7000.0 nm
Specimen HolderModel: FEI TITAN KRIOS AUTOGRID HOLDER
CameraDetector: GATAN K2 SUMMIT (4k x 4k)

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Image processing

ProcessingMethod: electron tomography / Number of sections: 59
3D reconstructionSoftware: eTomo / Resolution method: OTHER

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