[English] 日本語
Yorodumi
- EMDB-65519: in situ Tspan-7 spiral structure in cellular retraction fiber -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-65519
Titlein situ Tspan-7 spiral structure in cellular retraction fiber
Map dataAuthor claim: The reconstruction corresponds to a sub-tomogram average (STA) of a continuous filamentous assembly generated prior to single-particle helical reconstruction and local refinement. Due to the intrinsic helical and axial continuity of the specimen, adjacent sub-tomograms are not statistically independent, even after particle picking with a 60 A step size that approximates the helical rise and includes intentional redundancy reduction along the filament axis. Under these conditions, the STA dataset contains inherent sampling overlap, and residual correlations at long spatial frequencies are therefore expected. As a result, the FSC curve does not decay to zero as observed in reconstructions based on independent particle sampling. This behavior is a known consequence of overlapping sampling in filamentous STA workflows and does not indicate overfitting. Importantly, this reconstruction is not used for final structural interpretation or model building. It serves strictly as an intermediate reference for downstream single-particle helical reconstruction and local refinement. No atomic model was built on this map, and no structural claims are derived from it. To avoid misinterpretation, we have clarified in the Methods that this represents a redundancy-inherent, non-independent STA intermediate generated from a continuous filamentous assembly, and we have omitted the associated resolution statement.
Sample
  • Cell: in situ Tspan-7 spiral in cellular retraction fibers
KeywordsMembrane curvature / cell protrusion / helical structure / MEMBRANE PROTEIN
Biological speciesRattus norvegicus (Norway rat)
Methodsubtomogram averaging / cryo EM / Resolution: 16.0 Å
AuthorsJia X / Wang DJ / Li XP / Liu N / Yu L / Wang HW
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Vita / Year: 2026
Title: Polymerization of tetraspanin 7 into helical transmembrane skeletons for
Authors: Wang D / Jia X / Dharan R / Ren J / Zheng Y / Li X / Huang M / Xu K / Zhang Q / Sho T / Liu S / Yang F / Zhang QC / Sorkin R / Liu N / Wang HW / Yu L
History
DepositionJul 24, 2025-
Header (metadata) releaseJul 8, 2026-
Map releaseJul 8, 2026-
UpdateJul 8, 2026-
Current statusJul 8, 2026Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileReleased
AnnotationAuthor claim: The reconstruction corresponds to a sub-tomogram average (STA) of a continuous filamentous assembly generated prior to single-particle helical reconstruction and local refinement. Due to the intrinsic helical and axial continuity of the specimen, adjacent sub-tomograms are not statistically independent, even after particle picking with a 60 A step size that approximates the helical rise and includes intentional redundancy reduction along the filament axis. Under these conditions, the STA dataset contains inherent sampling overlap, and residual correlations at long spatial frequencies are therefore expected. As a result, the FSC curve does not decay to zero as observed in reconstructions based on independent particle sampling. This behavior is a known consequence of overlapping sampling in filamentous STA workflows and does not indicate overfitting. Importantly, this reconstruction is not used for final structural interpretation or model building. It serves strictly as an intermediate reference for downstream single-particle helical reconstruction and local refinement. No atomic model was built on this map, and no structural claims are derived from it. To avoid misinterpretation, we have clarified in the Methods that this represents a redundancy-inherent, non-independent STA intermediate generated from a continuous filamentous assembly, and we have omitted the associated resolution statement.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
5.44 Å/pix.
x 100 pix.
= 544. Å
5.44 Å/pix.
x 100 pix.
= 544. Å
5.44 Å/pix.
x 100 pix.
= 544. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 5.44 Å
Density
Contour LevelBy AUTHOR: 0.81
Minimum - Maximum-0.5912206 - 1.3393049
Average (Standard dev.)0.03845553 (±0.28973588)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions100100100
Spacing100100100
CellA=B=C: 544.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_65519_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_65519_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_65519_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : in situ Tspan-7 spiral in cellular retraction fibers

EntireName: in situ Tspan-7 spiral in cellular retraction fibers
Components
  • Cell: in situ Tspan-7 spiral in cellular retraction fibers

-
Supramolecule #1: in situ Tspan-7 spiral in cellular retraction fibers

SupramoleculeName: in situ Tspan-7 spiral in cellular retraction fibers / type: cell / ID: 1 / Parent: 0
Source (natural)Organism: Rattus norvegicus (Norway rat)

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation statecell

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281.15 K

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 3.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 5.5 µm / Nominal defocus min: 4.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Final reconstructionApplied symmetry - Point group: C7 (7 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 16.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0) / Number subtomograms used: 3572
ExtractionNumber tomograms: 114 / Number images used: 11355 / Software - Name: Warp
CTF correctionType: NONE
Final angle assignmentType: NOT APPLICABLE

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more