[English] 日本語
Yorodumi
- EMDB-52172: Dynactin pointed end in complex with NuMA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-52172
TitleDynactin pointed end in complex with NuMA
Map data
Sample
  • Complex: Dynein-Dynactin-NuMA-LIS1 complex
    • Complex: Dynactin
    • Complex: NuMA
    • Complex: Dynein-A and Dynein-B
Keywordsmotor protein / transport
Biological speciesSus scrofa (pig) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.78 Å
Authorsd'Amico EA / Carter AP
Funding support United Kingdom, 4 items
OrganizationGrant numberCountry
Wellcome Trust227434/Z/23/Z United Kingdom
Wellcome Trust210711/Z/18/Z United Kingdom
Medical Research Council (MRC, United Kingdom)MC_UP_A025_1011 United Kingdom
UK Research and Innovation (UKRI)EP/Y026004/1 United Kingdom
CitationJournal: To Be Published
Title: Structural and functional insights into activation and regulation of the dynein-dynactin-NuMA complex
Authors: Aslan M / d'Amico EA / Cho N / Taheri A / Zhao Y / Zhong J / Blaauw M / Carter AP / Dumont S / Yildiz A
History
DepositionNov 21, 2024-
Header (metadata) releaseDec 3, 2025-
Map releaseDec 3, 2025-
UpdateDec 3, 2025-
Current statusDec 3, 2025Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

emd_52172.png

Downloads & links

-
Map

FileDownload / File: emd_52172.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.8 Å/pix.
x 400 pix.
= 720. Å		1.8 Å/pix.
x 400 pix.
= 720. Å		1.8 Å/pix.
x 400 pix.
= 720. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.8 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.45
Minimum - Maximum-1.3895422 - 2.6790383
Average (Standard dev.)0.0067895544 (±0.06927112)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 720.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #2

Fileemd_52172_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #1

Fileemd_52172_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : Dynein-Dynactin-NuMA-LIS1 complex

EntireName: Dynein-Dynactin-NuMA-LIS1 complex
Components
  • Complex: Dynein-Dynactin-NuMA-LIS1 complex
    • Complex: Dynactin
    • Complex: NuMA
    • Complex: Dynein-A and Dynein-B

-
Supramolecule #1: Dynein-Dynactin-NuMA-LIS1 complex

SupramoleculeName: Dynein-Dynactin-NuMA-LIS1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #2-#9, #16, #10-#13, #1, #14-#15

-
Supramolecule #2: Dynactin

SupramoleculeName: Dynactin / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #3-#9, #16, #10-#12
Source (natural)Organism: Sus scrofa (pig)

-
Supramolecule #3: NuMA

SupramoleculeName: NuMA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Homo sapiens (human)

-
Supramolecule #4: Dynein-A and Dynein-B

SupramoleculeName: Dynein-A and Dynein-B / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #13, #1, #14-#15
Source (natural)Organism: Homo sapiens (human)

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 6.78 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 8092
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
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