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- EMDB-66970: human ORAI1 in C2 symmetry -

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Basic information

Entry
Database: EMDB / ID: EMD-66970
Titlehuman ORAI1 in C2 symmetry
Map data
Sample
  • Complex: human orai1
Keywordshuman / ORAI1 / calcium / ion channel / MEMBRANE PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.52 Å
AuthorsChen L / Wang Y / Zhang Y
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31821091 China
CitationJournal: PLoS One / Year: 2026
Title: Structural dynamics of the human Orai1 channel revealed by cryo-electron microscopy.
Authors: Yiming Zhang / Yuan Wang / Jindou Liu / Weiwei Bei / Hongkun Wang / Junli Wang / Lei Chen / Youjun Wang /
Abstract: The pore-forming Orai1 protein is an essential component of store-operated calcium entry (SOCE), a process vital to diverse cellular and physiological functions. Mutations in human Orai1 cause severe ...The pore-forming Orai1 protein is an essential component of store-operated calcium entry (SOCE), a process vital to diverse cellular and physiological functions. Mutations in human Orai1 cause severe immunodeficiencies and myopathies, yet structural insights have remained largely elusive. To address this, we studied the structure of detergent-solubilized human Orai1 (hOrai1) by cryo-electron microscopy. While the overall resolution is moderate, the reconstructed map confirms a conserved hexameric architecture and enables assignment of transmembrane helices. We observed profound structural heterogeneity, with particles adopting both C6- and C2-symmetric conformations, indicative of dynamic rearrangements. This study establishes a framework for future structural and mechanistic studies of hOrai1.
History
DepositionNov 6, 2025-
Header (metadata) releaseSep 9, 2026-
Map releaseSep 9, 2026-
UpdateSep 9, 2026-
Current statusSep 9, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_66970.png

Downloads & links

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Map

FileDownload / File: emd_66970.map.gz / Format: CCP4 / Size: 22.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.5 Å/pix.
x 180 pix.
= 270. Å		1.5 Å/pix.
x 180 pix.
= 270. Å		1.5 Å/pix.
x 180 pix.
= 270. Å

Surface

Projections

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.5 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.92
Minimum - Maximum-2.2682397 - 3.2624438
Average (Standard dev.)0.00016588155 (±0.08895187)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions180180180
Spacing180180180
CellA=B=C: 270.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_66970_msk_1.map
Projections & Slices
AxesZYX

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Additional map: #1

Fileemd_66970_additional_1.map
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Half map: #1

Fileemd_66970_half_map_1.map
Projections & Slices
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Half map: #2

Fileemd_66970_half_map_2.map
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Sample components

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Entire : human orai1

EntireName: human orai1
Components
  • Complex: human orai1

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Supramolecule #1: human orai1

SupramoleculeName: human orai1 / type: complex / ID: 1 / Parent: 0
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: 6.3
VitrificationCryogen name: ETHANE / Chamber humidity: 100 %

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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: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.52 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 26047
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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