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- EMDB-46429: Consensus force-activated alpha-catenin-F-actin complex -

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Basic information

Entry
Database: EMDB / ID: EMD-46429
TitleConsensus force-activated alpha-catenin-F-actin complex
Map dataMain map for consensus alpha-catenin bound F-actin under myosin forces
Sample
  • Complex: Consensus alpha-catenin bound F-actin under myosin-directed force conditions
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Catenin Alpha 1
KeywordsCytoskeleton / actin / STRUCTURAL PROTEIN
Biological speciesGallus gallus (chicken) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 10.4 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

Downloads & links

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Map

FileDownload / File: emd_46429.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMain map for consensus alpha-catenin bound F-actin under myosin forces
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.66 Å/pix.
x 384 pix.
= 1021.44 Å
2.66 Å/pix.
x 384 pix.
= 1021.44 Å
2.66 Å/pix.
x 384 pix.
= 1021.44 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.66 Å
Density
Contour LevelBy AUTHOR: 1.0
Minimum - Maximum-0.9164305 - 2.928741
Average (Standard dev.)0.0006277209 (±0.10026119)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 1021.44006 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_46429_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: Half map 1 for consensus alpha-catenin bound F-actin...

Fileemd_46429_half_map_1.map
AnnotationHalf map 1 for consensus alpha-catenin bound F-actin under myosin forces
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: Half map 2 for consensus alpha-catenin bound F-actin...

Fileemd_46429_half_map_2.map
AnnotationHalf map 2 for consensus alpha-catenin bound F-actin under myosin forces
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Consensus alpha-catenin bound F-actin under myosin-directed force...

EntireName: Consensus alpha-catenin bound F-actin under myosin-directed force conditions
Components
  • Complex: Consensus alpha-catenin bound F-actin under myosin-directed force conditions
    • Protein or peptide: Actin, alpha skeletal muscle
    • Protein or peptide: Catenin Alpha 1

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Supramolecule #1: Consensus alpha-catenin bound F-actin under myosin-directed force...

SupramoleculeName: Consensus alpha-catenin bound F-actin under myosin-directed force conditions
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

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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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Macromolecule #2: Catenin Alpha 1

MacromoleculeName: Catenin Alpha 1 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MTAVHAGNIN FKWDPKSLE I RTLAVERL LE PLVTQVT TLV NTNSKG PSNK KRGRS KKAHV LAAS VEQATE NFL EKGDKIA KE SQFLKEEL V AAVEDVRKQ GDLMKAAAGE FADDPCSSV K RGNMVRAA RA LLSAVTR LLI LADMAD VYKL LVQLK ...String:
MTAVHAGNIN FKWDPKSLE I RTLAVERL LE PLVTQVT TLV NTNSKG PSNK KRGRS KKAHV LAAS VEQATE NFL EKGDKIA KE SQFLKEEL V AAVEDVRKQ GDLMKAAAGE FADDPCSSV K RGNMVRAA RA LLSAVTR LLI LADMAD VYKL LVQLK VVEDG ILKL RNAGNE QDL GIQYKAL KP EVDKLNIM A AKRQQELKD VGHRDQMAAA RGILQKNVP I LYTASQAC LQ HPDVAAY KAN RDLIYK QLQQ AVTGI SNAAQ ATAS DDASQH QGG GGGELAY AL NNFDKQII V DPLSFSEER FRPSLEERLE SIISGAALM A DSSCTRDD RR ERIVAEC NAV RQALQD LLSE YMGNA GRKER SDAL NSAIDK MTK KTRDLRR QL RKAVMDHV S DSFLETNVP LLVLIEAAKN GNEKEVKEY A QVFREHAN KL IEVANLA CSI SNNEEG VKLV RMSAS QLEAL CPQV INAALA LAA KPQSKLA QE NMDLFKEQ W EKQVRVLTD AVDDITSIDD FLAVSENHI L EDVNKCVI AL QEKDVDG LDR TAGAIR GRAA RVIHV VTSEM DNYE PGVYTE KVL EATKLLS NT VMPRFTEQ V EAAVEALSS DPAQPMDENE FIDASRLVY D GIRDIRKA VL MIRTPEE LDD SDFETE DFDV RSRTS VQTED DQLI AGQSAR AIM AQLPQEQ KA KIAEQVAS F QEEKSKLDA EVSKWDDSGN DIIVLAKQM C MIMMEMTD FT RGKGPLK NTS DVISAA KKIA EAGSR MDKLG RTIA DHCPDS ACK QDLLAYL QR IALYCHQL N ICSKVKAEV QNLGGELVVS GVDSAMSLI Q AAKNLMNA VV QTVKASY VAS TKYQKS QGMA SLNLP AVSWK MKAP EKKPLV KRE KQDETQT KI KRASQKKH V NPVQALSEF KAMDSI

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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 K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 56.33 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: 22500
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: 10.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 3289
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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