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- EMDB-46428: Control myosin-tethered F-actin -ATP 2 -

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Basic information

Entry
Database: EMDB / ID: EMD-46428
TitleControl myosin-tethered F-actin -ATP 2
Map dataAverage map of second subset of no ATP control dual motor conditions
Sample
  • Complex: Asymmetric reconstruction of F-actin tethered by myosin motors without ATP, subset 2
    • Protein or peptide: Actin, alpha skeletal muscle
KeywordsCytoskeleton / actin / STRUCTURAL PROTEIN
Biological speciesGallus gallus (chicken)
Methodsingle particle reconstruction / cryo EM / Resolution: 8.9 Å
AuthorsReynolds MJ / Carl AG / Alushin GM
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM141044 United States
CitationJournal: To be published
Title: Myosin forces elicit an F-actin structural landscape that modulates mechanosensitive protein recognition
Authors: Carl AG / Reynolds MJ / Gurel PS / Phua DYZ / Sun X / Mei L / Hamilton K / Takagi Y / Noble AJ / Sellers JR / Alushin GM
History
DepositionAug 5, 2024-
Header (metadata) releaseAug 13, 2025-
Map releaseAug 13, 2025-
UpdateAug 13, 2025-
Current statusAug 13, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_46428.png

Downloads & links

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Map

FileDownload / File: emd_46428.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationAverage map of second subset of no ATP control dual motor conditions
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.88 Å/pix.
x 384 pix.
= 1105.92 Å		2.88 Å/pix.
x 384 pix.
= 1105.92 Å		2.88 Å/pix.
x 384 pix.
= 1105.92 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.88 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.5
Minimum - Maximum-0.8852032 - 3.5767143
Average (Standard dev.)-0.033454124 (±0.12508643)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 1105.92 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_46428_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 1 of second subset of no ATP control dual motor conditions

Fileemd_46428_half_map_1.map
AnnotationHalf-map 1 of second subset of no ATP control dual motor conditions
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 2 of second subset of no ATP control dual motor conditions

Fileemd_46428_half_map_2.map
AnnotationHalf-map 2 of second subset of no ATP control dual motor conditions
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Asymmetric reconstruction of F-actin tethered by myosin motors wi...

EntireName: Asymmetric reconstruction of F-actin tethered by myosin motors without ATP, subset 2
Components
  • Complex: Asymmetric reconstruction of F-actin tethered by myosin motors without ATP, subset 2
    • Protein or peptide: Actin, alpha skeletal muscle

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Supramolecule #1: Asymmetric reconstruction of F-actin tethered by myosin motors wi...

SupramoleculeName: Asymmetric reconstruction of F-actin tethered by myosin motors without ATP, subset 2
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Gallus gallus (chicken)

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Macromolecule #1: Actin, alpha skeletal muscle

MacromoleculeName: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Gallus gallus (chicken)
SequenceString: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY ...String:
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY EGYALPHAIM RLDLAGRDLT DYLMKILTER GYSFVTTAER EIVRDIKEKL CYVALDFENE MATAASSS S LEKSYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVMSGGTTM YPGIADRMQ KEITALAPST MKIKIIAPPE RKYSVWIGGS ILASLSTFQQ MWITKQEYDE AGPSIVHRKC F

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 59.156 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 64000
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
Details: Ab initio reconstruction as implemented in cryoSPARC
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 8.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 3137
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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