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- EMDB-18981: Structure of the human UAP56 RecA1 RecA2 - TREX-2 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-18981
TitleStructure of the human UAP56 RecA1 RecA2 - TREX-2 complex
Map dataStructure of the human UAP56 RecA1 RecA2 - TREX-2 complex, map.
Sample
  • Complex: Human UAP56 - TREX-2 complex
    • Complex: Human TREX-2 complex middle domain
KeywordsmRNA export / nuclear pore basket / GENE REGULATION
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.22 Å
AuthorsHohmann U / Graf M / Plaschka C
Funding supportEuropean Union, 3 items
OrganizationGrant numberCountry
European Research Council (ERC)949081European Union
H2020 Marie Curie Actions of the European Commission896416European Union
European Molecular Biology Organization (EMBO)ALTF_1175-2019European Union
CitationJournal: To Be Published
Title: A molecular switch orchestrates the export of human messenger RNA
Authors: Hohmann U / Graf M / Brennecke J / Plaschka C
History
DepositionNov 25, 2023-
Header (metadata) releaseJun 11, 2025-
Map releaseJun 11, 2025-
UpdateJun 11, 2025-
Current statusJun 11, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18981.png

Downloads & links

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Map

FileDownload / File: emd_18981.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationStructure of the human UAP56 RecA1 RecA2 - TREX-2 complex, map.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.88 Å/pix.
x 256 pix.
= 224.512 Å		0.88 Å/pix.
x 256 pix.
= 224.512 Å		0.88 Å/pix.
x 256 pix.
= 224.512 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.877 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.049
Minimum - Maximum-0.306974 - 0.45010293
Average (Standard dev.)0.00045245717 (±0.015399795)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 224.512 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Structure of the human UAP56 RecA1 RecA2 -...

Fileemd_18981_half_map_1.map
AnnotationStructure of the human UAP56 RecA1 RecA2 - TREX-2 complex, half map A.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Structure of the human UAP56 RecA1 RecA2 -...

Fileemd_18981_half_map_2.map
AnnotationStructure of the human UAP56 RecA1 RecA2 - TREX-2 complex, half map B.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human UAP56 - TREX-2 complex

EntireName: Human UAP56 - TREX-2 complex
Components
  • Complex: Human UAP56 - TREX-2 complex
    • Complex: Human TREX-2 complex middle domain

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Supramolecule #1: Human UAP56 - TREX-2 complex

SupramoleculeName: Human UAP56 - TREX-2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: Human TREX-2 complex middle domain

SupramoleculeName: Human TREX-2 complex middle domain / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.7 mg/mL
BufferpH: 7.9
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 281 K / Instrument: LEICA EM GP

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.22 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 7412
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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