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- EMDB-70139: Phycoerythrin bound by 1C5H TCR (complex consensus map) -

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Basic information

Entry
Database: EMDB / ID: EMD-70139
TitlePhycoerythrin bound by 1C5H TCR (complex consensus map)
Map dataPhycoerythrin bound by 1C5H TCR (complex consensus map)
Sample
  • Complex: 1C5H TCR bound to R-phycoerythrin
    • Complex: R-phycoerythrin
    • Complex: 1C5H TCR
KeywordsT-cell / gamma delta TCR / phycoerythrin / direct / IMMUNE SYSTEM
Biological speciesHomo sapiens (human) / Ceramium secundatum (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.03 Å
AuthorsRashleigh L / Venugopal H / Rossjohn J / Gully BS
Funding support Australia, 1 items
OrganizationGrant numberCountry
Australian Research Council (ARC)DP230102073 Australia
CitationJournal: Structure / Year: 2025
Title: Antibody-like recognition of a gamma delta T cell receptor toward a foreign antigen
Authors: Rashleigh L / Venugopal H / Rice MT / Gunasinghe SD / Sok CL / Gherardin NA / Almeida CF / Van Rhijn I / Moody DB / Godfrey DI / Rossjohn J / Gully BS
History
DepositionApr 10, 2025-
Header (metadata) releaseAug 6, 2025-
Map releaseAug 6, 2025-
UpdateAug 6, 2025-
Current statusAug 6, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_70139.png

Downloads & links

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Map

FileDownload / File: emd_70139.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPhycoerythrin bound by 1C5H TCR (complex consensus map)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 360 pix.
= 295.2 Å		0.82 Å/pix.
x 360 pix.
= 295.2 Å		0.82 Å/pix.
x 360 pix.
= 295.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.49062356 - 1.2610503
Average (Standard dev.)0.00047629047 (±0.042907324)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 295.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_70139_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Additional Map

Fileemd_70139_additional_1.map
AnnotationAdditional Map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map A

Fileemd_70139_half_map_1.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map A

Fileemd_70139_half_map_2.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : 1C5H TCR bound to R-phycoerythrin

EntireName: 1C5H TCR bound to R-phycoerythrin
Components
  • Complex: 1C5H TCR bound to R-phycoerythrin
    • Complex: R-phycoerythrin
    • Complex: 1C5H TCR

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Supramolecule #1: 1C5H TCR bound to R-phycoerythrin

SupramoleculeName: 1C5H TCR bound to R-phycoerythrin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: R-phycoerythrin

SupramoleculeName: R-phycoerythrin / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2
Source (natural)Organism: Ceramium secundatum (eukaryote)

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Supramolecule #3: 1C5H TCR

SupramoleculeName: 1C5H TCR / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3-#4
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

BufferpH: 8.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.4 µm
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: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.03 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 45513
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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