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- EMDB-47023: CryoEM structure of the Salpingoeca rosetta caveolin complex -

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Basic information

Entry
Database: EMDB / ID: EMD-47023
TitleCryoEM structure of the Salpingoeca rosetta caveolin complex
Map dataSalpingoeca rosetta caveolin complex
Sample
  • Complex: S. rosetta caveolin complex
    • Protein or peptide: Caveolin
KeywordsMembrane-shaping protein / monotonic membrane protein / MEMBRANE PROTEIN
Function / homologyCaveolin / Caveolin / caveola assembly / caveola / molecular adaptor activity / Golgi membrane / Caveolin
Function and homology information
Biological speciesSalpingoeca rosetta (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsConnolly SM / Ohi MD
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM151635 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01HL144131 United States
CitationJournal: To Be Published
Title: Evolutionarily diverse caveolins share a common structural framework build around amphipathic discs
Authors: Han B / Connolly SM / Wilson LFL / Schultz D / Gulsevin A / Meiler J / Karakas E / Ohi MD / Kenworthy AK
History
DepositionSep 16, 2024-
Header (metadata) releaseJul 9, 2025-
Map releaseJul 9, 2025-
UpdateJul 9, 2025-
Current statusJul 9, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_47023.png

Downloads & links

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Map

FileDownload / File: emd_47023.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSalpingoeca rosetta caveolin complex
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.87 Å/pix.
x 320 pix.
= 277.44 Å		0.87 Å/pix.
x 320 pix.
= 277.44 Å		0.87 Å/pix.
x 320 pix.
= 277.44 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.867 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.029
Minimum - Maximum-0.10132323 - 0.20352994
Average (Standard dev.)0.00089664385 (±0.00593988)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 277.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Salpingoeca rosetta caveolin complex half map A

Fileemd_47023_half_map_1.map
AnnotationSalpingoeca rosetta caveolin complex half map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Salpingoeca rosetta caveolin complex half map B

Fileemd_47023_half_map_2.map
AnnotationSalpingoeca rosetta caveolin 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 : S. rosetta caveolin complex

EntireName: S. rosetta caveolin complex
Components
  • Complex: S. rosetta caveolin complex
    • Protein or peptide: Caveolin

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Supramolecule #1: S. rosetta caveolin complex

SupramoleculeName: S. rosetta caveolin complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Salpingoeca rosetta (eukaryote)

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Macromolecule #1: Caveolin

MacromoleculeName: Caveolin / type: protein_or_peptide / ID: 1 / Number of copies: 11 / Enantiomer: LEVO
Source (natural)Organism: Salpingoeca rosetta (eukaryote)
Molecular weightTheoretical: 25.605049 KDa
Recombinant expressionOrganism: Escherichia coli BL21 (bacteria)
SequenceString: MSYHKENTPL TAGSQAASSS TASYQTPPYA PPSSVNHQQQ QQARAAAPSY VGPTPTSTTT YPTIFTPGGF GAPPPSDPEA EEKYIERQL KYLGPISQVS DAYRLDTTTL KIEFDDSFPE VSKPGPALES VRKLNRILYE GMSDAIHIIF SLFLGFLAAI T VGFFMGMA ...String:
MSYHKENTPL TAGSQAASSS TASYQTPPYA PPSSVNHQQQ QQARAAAPSY VGPTPTSTTT YPTIFTPGGF GAPPPSDPEA EEKYIERQL KYLGPISQVS DAYRLDTTTL KIEFDDSFPE VSKPGPALES VRKLNRILYE GMSDAIHIIF SLFLGFLAAI T VGFFMGMA RFMYTYMAGP FNQLMFLLIA SLAPSWRAFF RAGMDPIFES GSLALSNIQV RLGMEGKARH KELKD

UniProtKB: Caveolin

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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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Average electron dose: 59.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 105000
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 reconstructionApplied symmetry - Point group: C11 (11 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 66202
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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