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- EMDB-46849: structure of dynactin, dynein tail with TRAK2 from dynein-dynacti... -

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Basic information

Entry
Database: EMDB / ID: EMD-46849
Titlestructure of dynactin, dynein tail with TRAK2 from dynein-dynactin-TRAK2 on microtubules
Map datastructure of dynactin, dynein tail with TRAK2 from dynein-dynactin-TRAK2 on microtubules
Sample
  • Complex: Dynactin, dynein tail with TRAK2 of dynein-dynactin-TRAK2 complex on microtubules
    • Protein or peptide: x 14 types
  • Ligand: x 3 types
Keywordsdynein / TRAK2 / dynactin / microtubule / MOTOR PROTEIN
Function / homology
Function and homology information


RHOT1 GTPase cycle / RHOT2 GTPase cycle / mitochondrion distribution / dendritic transport of mitochondrion / Advanced glycosylation endproduct receptor signaling / retrograde axonal transport of mitochondrion / negative regulation of axonogenesis / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions ...RHOT1 GTPase cycle / RHOT2 GTPase cycle / mitochondrion distribution / dendritic transport of mitochondrion / Advanced glycosylation endproduct receptor signaling / retrograde axonal transport of mitochondrion / negative regulation of axonogenesis / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / RHOF GTPase cycle / Formation of the canonical BAF (cBAF) complex / Formation of the polybromo-BAF (pBAF) complex / Formation of the embryonic stem cell BAF (esBAF) complex / Formation of the non-canonical BAF (ncBAF) complex / GBP-mediated host defense / sterol sensor activity / Platelet degranulation / Gap junction degradation / Formation of annular gap junctions / UCH proteinases / dynactin complex / centriolar subdistal appendage / Clathrin-mediated endocytosis / centriole-centriole cohesion / positive regulation of neuromuscular junction development / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / Recruitment of mitotic centrosome proteins and complexes / microtubule anchoring at centrosome / F-actin capping protein complex / WASH complex / Regulation of CDH1 Function / Formation of the dystrophin-glycoprotein complex (DGC) / lysosome to ER cholesterol transport / ventral spinal cord development / retromer complex / cytoskeleton-dependent cytokinesis / dynein complex / microtubule plus-end / mitotic nuclear membrane disassembly / protein O-linked glycosylation / positive regulation of microtubule nucleation / cellular response to cytochalasin B / regulation of transepithelial transport / dendrite morphogenesis / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / GABA receptor binding / protein localization to adherens junction / non-motile cilium assembly / barbed-end actin filament capping / dense body / Neutrophil degranulation / Tat protein binding / motor behavior / postsynaptic actin cytoskeleton / vesicle transport along microtubule / apical protein localization / neuron cellular homeostasis / retrograde transport, endosome to Golgi / adherens junction assembly / neuromuscular process / minus-end-directed microtubule motor activity / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / microtubule associated complex / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / dynein light intermediate chain binding / cytoplasmic dynein complex / MHC class II antigen presentation / nuclear migration / Recruitment of NuMA to mitotic centrosomes / tight junction / COPI-mediated anterograde transport / microtubule-based movement / apical junction complex / intercellular bridge / myosin binding / endosome to lysosome transport / establishment of mitotic spindle orientation / TPR domain binding / dynein intermediate chain binding / NuA4 histone acetyltransferase complex / regulation of norepinephrine uptake / transporter regulator activity / cell leading edge / cortical cytoskeleton / cleavage furrow / establishment or maintenance of cell polarity / microtubule organizing center / neuromuscular junction development / nitric-oxide synthase binding
Similarity search - Function
HAP1, N-terminal / Trafficking kinesin-binding protein, C-terminal / : / HAP1 N-terminal conserved region / Kinesin associated protein / Kinesin associated protein / HAP1 N-terminal conserved region / Dynactin subunit 3 / Dynactin subunit p22 / Dynactin subunit 4 ...HAP1, N-terminal / Trafficking kinesin-binding protein, C-terminal / : / HAP1 N-terminal conserved region / Kinesin associated protein / Kinesin associated protein / HAP1 N-terminal conserved region / Dynactin subunit 3 / Dynactin subunit p22 / Dynactin subunit 4 / Dynactin p62 family / Dynamitin / Dynamitin / Dynactin subunit 6 / : / Domain of unknown function (DUF8221) / Dynein associated protein / Dynein associated protein / : / Dynactin subunit 5 / Cytoplasmic dynein 1 intermediate chain 1/2 / Cytoplasmic dynein 1 intermediate chain 2 / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / : / CAP-Gly domain signature. / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain / CAP-Gly domain profile. / CAP_GLY / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / : / Dynein heavy chain, ATPase lid domain / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / P-loop containing dynein motor region / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, linker / Dynein heavy chain, AAA module D4 / Dynein heavy chain, coiled coil stalk / Dynein heavy chain / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain, linker, subdomain 3 / Dynein heavy chain, AAA1 domain, small subdomain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, N-terminal region 2 / Hydrolytic ATP binding site of dynein motor region / Microtubule-binding stalk of dynein motor / P-loop containing dynein motor region D4 / ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Trimeric LpxA-like superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Dynactin subunit 5 / Dynactin subunit 1 / Cytoplasmic dynein 1 heavy chain 1 / Dynactin subunit 4 / Cytoplasmic dynein 1 intermediate chain 2 / Dynactin subunit 2 / Actin related protein 1A / F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Dynactin subunit 6 ...Dynactin subunit 5 / Dynactin subunit 1 / Cytoplasmic dynein 1 heavy chain 1 / Dynactin subunit 4 / Cytoplasmic dynein 1 intermediate chain 2 / Dynactin subunit 2 / Actin related protein 1A / F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Dynactin subunit 6 / Dynactin subunit 3 / Actin-related protein 10 / Trafficking protein, kinesin binding 2 / Actin, cytoplasmic 1
Similarity search - Component
Biological speciesSus scrofa (pig) / Mus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 8.8 Å
AuthorsRao Q / Chai P / Zhang K
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM142959 United States
CitationJournal: bioRxiv / Year: 2024
Title: Molecular basis for the assembly of the dynein transport machinery on microtubules.
Authors: Qinhui Rao / Pengxin Chai / Kai Zhang /
Abstract: Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has ...Cytoplasmic dynein-1, a microtubule-based motor protein, requires dynactin and an adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The role of microtubules in DDA assembly has been elusive. Here, we reveal detailed structural insights into microtubule-mediated DDA assembly using cryo-electron microscopy. We find that an adaptor-independent dynein-dynactin complex (DD) predominantly forms on microtubules in an intrinsic 2:1 stoichiometry, induced by spontaneous parallelization of dynein upon microtubule binding. Adaptors can squeeze in and exchange within the assembled microtubule-bound DD complex, which is enabled by relative rotations between dynein and dynactin, and further facilitated by dynein light intermediate chains that assist in an adaptor 'search' mechanism. Our findings elucidate the dynamic adaptability of the dynein transport machinery, and reveal a new mode for assembly of the motile complex.
History
DepositionSep 3, 2024-
Header (metadata) releaseSep 10, 2025-
Map releaseSep 10, 2025-
UpdateMay 13, 2026-
Current statusMay 13, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_46849.png

Downloads & links

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Map

FileDownload / File: emd_46849.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationstructure of dynactin, dynein tail with TRAK2 from dynein-dynactin-TRAK2 on microtubules
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
3.3 Å/pix.
x 192 pix.
= 633.6 Å		3.3 Å/pix.
x 192 pix.
= 633.6 Å		3.3 Å/pix.
x 192 pix.
= 633.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 3.3 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-0.29642594 - 1.1871856
Average (Standard dev.)-0.00778094 (±0.05149311)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 633.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: half map

Fileemd_46849_half_map_1.map
Annotationhalf map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map

Fileemd_46849_half_map_2.map
Annotationhalf map
Projections & Slices
AxesZYX

Projections

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Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Dynactin, dynein tail with TRAK2 of dynein-dynactin-TRAK2 complex...

EntireName: Dynactin, dynein tail with TRAK2 of dynein-dynactin-TRAK2 complex on microtubules
Components
  • Complex: Dynactin, dynein tail with TRAK2 of dynein-dynactin-TRAK2 complex on microtubules
    • Protein or peptide: Alpha-centractin
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Actin-related protein 10
    • Protein or peptide: F-actin-capping protein subunit alpha-1
    • Protein or peptide: F-actin-capping protein subunit beta
    • Protein or peptide: Dynactin subunit 2
    • Protein or peptide: Dynactin subunit 3
    • Protein or peptide: Dynactin subunit 6
    • Protein or peptide: Dynactin subunit 5
    • Protein or peptide: Dynactin subunit 1
    • Protein or peptide: Dynactin subunit 4
    • Protein or peptide: Trafficking protein, kinesin binding 2
    • Protein or peptide: Cytoplasmic dynein 1 heavy chain 1
    • Protein or peptide: Cytoplasmic dynein 1 intermediate chain 2
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ZINC ION

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Supramolecule #1: Dynactin, dynein tail with TRAK2 of dynein-dynactin-TRAK2 complex...

SupramoleculeName: Dynactin, dynein tail with TRAK2 of dynein-dynactin-TRAK2 complex on microtubules
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#14
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 5 MDa

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Macromolecule #1: Alpha-centractin

MacromoleculeName: Alpha-centractin / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 42.670688 KDa
SequenceString: MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP KAEEHRGLLS IRYPMEHGIV KDWNDMERI WQYVYSKDQL QTFSEEHPVL LTEAPLNPRK NRERAAEVFF ETFNVPALFI SMQAVLSLYA TGRTTGVVLD S GDGVTHAV ...String:
MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP KAEEHRGLLS IRYPMEHGIV KDWNDMERI WQYVYSKDQL QTFSEEHPVL LTEAPLNPRK NRERAAEVFF ETFNVPALFI SMQAVLSLYA TGRTTGVVLD S GDGVTHAV PIYEGFAMPH SIMRIDIAGR DVSRFLRLYL RKEGYDFHSS SEFEIVKAIK ERACYLSINP QKDETLETEK AQ YYLPDGS TIEIGPSRFR APELLFRPDL IGEESEGIHE VLVFAIQKSD MDLRRTLFSN IVLSGGSTLF KGFGDRLLSE VKK LAPKDV KIRISAPQER LYSTWIGGSI LASLDTFKKM WVSKKEYEED GARSIHRKTF

UniProtKB: Actin related protein 1A

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Macromolecule #2: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 41.78266 KDa
SequenceString: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String:
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #3: Actin-related protein 10

MacromoleculeName: Actin-related protein 10 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 46.250785 KDa
SequenceString: MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKKAGMPK PIKVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VVIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG ...String:
MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKKAGMPK PIKVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VVIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG KALHKELETQ LLEQCTVDTG AAKEQSLPSV MGSIPEGVLE DIKVRTCFVS DLTRGLKIQA AKFNIDGNTE RP SPPPNVD YPLDGEKILH VLGSIRDSVV EILFEQDNEE KSVATLILDS LMQCPIDTRK QLAENLVIIG GTSMLPGFLH RLL AEIRYL VEKPKYKKTL GTKTFRIHTP PAKANCVAWL GGAIFGALQD ILGSRSVSKE YYNQTGRIPD WCSLNNPPLE MVFD VGKSQ PPLMKRAFST EK

UniProtKB: Actin-related protein 10

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Macromolecule #4: F-actin-capping protein subunit alpha-1

MacromoleculeName: F-actin-capping protein subunit alpha-1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 33.059848 KDa
SequenceString: MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEVDGSLKS WRESCDSALR AYVKDHYSNG FCTVYAKNID GQQTIIACIE S HQFQPKNF ...String:
MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEVDGSLKS WRESCDSALR AYVKDHYSNG FCTVYAKNID GQQTIIACIE S HQFQPKNF WNGRWRSEWK FTITPPTAQV VGVLKIQVHY YEDGNVQLVS HKDVQDSVTV SNEAQTAKEF IKIIEHAENE YQ TAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA

UniProtKB: F-actin-capping protein subunit alpha-1

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Macromolecule #5: F-actin-capping protein subunit beta

MacromoleculeName: F-actin-capping protein subunit beta / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 30.669768 KDa
SequenceString: MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMP SARLRKLEVE ANNAFDQYRD LYFEGGVSSV YLWDLDHGFA GVILIKKAGD GSKKIKGCWD SIHVVEVQEK S SGRTAHYK ...String:
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMP SARLRKLEVE ANNAFDQYRD LYFEGGVSSV YLWDLDHGFA GVILIKKAGD GSKKIKGCWD SIHVVEVQEK S SGRTAHYK LTSTVMLWLQ TNKSGSGTMN LGGSLTRQME KDETVSDCSP HIANIGRLVE DMENKIRSTL NEIYFGKTKD IV NGLRSVQ TFADKSKQEA LKNDLVEALK RKQQC

UniProtKB: F-actin-capping protein subunit beta

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Macromolecule #6: Dynactin subunit 2

MacromoleculeName: Dynactin subunit 2 / type: protein_or_peptide / ID: 6 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 44.704414 KDa
SequenceString: MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAELEEL TSTSVEHIIV NPNAAYDKFK DKRVGTKGLD FSDRIGKTKR TGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKMTVKES ATEEKLTPVV LAKQLAALKQ QLVASHLEKL L GPDAAINL ...String:
MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAELEEL TSTSVEHIIV NPNAAYDKFK DKRVGTKGLD FSDRIGKTKR TGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKMTVKES ATEEKLTPVV LAKQLAALKQ QLVASHLEKL L GPDAAINL TDPDGALAKR LLLQLEATKN TKGAGSGGKT TSGSPPDSSL VTYELHSRPE QDKFSQAAKV AELEKRLTEL EA TVRCDQD AQNPLSAGLQ GACLMETVEL LQAKVSALDL AVLDQVEARL QSVLGKVNEI AKHKASVEDA DTQSKVHQLY ETI QRWSPI ASTLPELVQR LVTIKQLHEQ AMQFGQLLTH LDTTQQMIAC SLKDNATLLT QVQTTMRENL STVEGNFANI DERM KKLGK

UniProtKB: Dynactin subunit 2

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Macromolecule #7: Dynactin subunit 3

MacromoleculeName: Dynactin subunit 3 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 21.192477 KDa
SequenceString:
MAGVTDVQRL QARLEELERW VYGPGGSRGS RKVADGLVKV QVALGNIASK RERVKILYKK IEDLIKYLDP EYMDRIAIPD ASKLQFILA EEQFILSQVA LLEQVEALVP MLDSAHIKAV PEHAARLQRL AQIHIQQQDQ CVEITEESKA LLEEYNKTTM L LSKQFVQW DELLCQLEAA KQVKPAEE

UniProtKB: Dynactin subunit 3

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Macromolecule #8: Dynactin subunit 6

MacromoleculeName: Dynactin subunit 6 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 20.70391 KDa
SequenceString:
MAEKTQKSVK IAPGAVVCVE SEIRGDVTIG PRTVIHPKAR IIAEAGPIVI GEGNLIEEQA LIINAHPDNI TPDAEDSEPK PMIIGTNNV FEVGCYSQAM KMGDNNVIES KAYVGRNVIL TSGCIIGACC NLNTFEVIPE NTVIYGADCL RRVQTERPQP Q TLQLDFLM KILPNYHHLK KTMKGSSTPV KN

UniProtKB: Dynactin subunit 6

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Macromolecule #9: Dynactin subunit 5

MacromoleculeName: Dynactin subunit 5 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 20.150533 KDa
SequenceString:
MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH CVVKSRSVIR PPFKKFSKGV AFFPLHIGD HVFIEEDCVV NAAQIGSYVH VGKNCVIGRR CVLKDCCKIL DNTVLPPETV VPPFTVFSGC PGLFSGELPE C TQELMIDV TKSYYQKFLP LTQV

UniProtKB: Dynactin subunit 5

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Macromolecule #10: Dynactin subunit 1

MacromoleculeName: Dynactin subunit 1 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 142.015484 KDa
SequenceString: MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLRR EGTDSNAKTS KLRGPKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG ...String:
MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFV RQSQIQVFED GADTTSPETP DSSASKVLRR EGTDSNAKTS KLRGPKPKKA PTARKTTTRR PKPTRPASTG V AGASSSLG PSGSASAGEL SSSEPSTPAQ TPLAAPIIPT PALTSPGAAP PLPSPSKEEE GLRAQVRDLE EKLETLRLKR AE DKAKLKE LEKHKIQLEQ VQEWKSKMQE QQADLQRRLK EARKEAKEAL EAKERYMEEM ADTADAIEMA TLDKEMAEER AES LQQEVE ALKERVDELT TDLEILKAEI EEKGSDGAAS SYQLKQLEEQ NARLKDALVR MRDLSSSEKQ EHVKLQKLME KKNQ ELEVV RQQRERLQEE LSQAESTIDE LKEQVDAALG AEEMVEMLTD RNLNLEEKVR ELRETVGDLE AMNEMNDELQ ENARE TELE LREQLDMAGA RVREAQKRVE AAQETVADYQ QTIKKYRQLT AHLQDVNREL TNQQEASVER QQQPPPETFD FKIKFA ETK AHAKAIEMEL RQMEVAQANR HMSLLTAFMP DSFLRPGGDH DCVLVLLLMP RLICKAELIR KQAQEKFDLS ENCSERP GL RGAAGEQLSF AAGLVYSLSL LQATLHRYEH ALSQCSVDVY KKVGSLYPEM SAHERSLDFL IELLHKDQLD ETVNVEPL T KAIKYYQHLY SIHLAEQPED STMQLADHIK FTQSALDCMS VEVGRLRAFL QGGQEASDIA LLLRDLETSC SDIRQFCKK IRRRMPGTDA PGIPAALAFG AQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGT PSSSPYECL RQSCNILIST MNKLATAMQE GEYDAERPPS KPPPVELRAA ALRAEITDAE GLGLKLEDRE TVIKELKKSL K IKGEELSE ANVRLSLLEK KLDSAAKDAD ERIEKVQTRL EETQALLRKK EKEFEETMDA LQADIDQLEA EKAELKQRLN SQ SKRTIEG IRGPPPSGIA TLVSGIAGEE QQRGGAPGQA PGIVPGPGLV KDSPLLLQQI SAMRLHISQL QHENSVLKGA QMK ASLAAL PPLHVAKLSL PPHEGPGSEL AAGALYRKTN QLLETLNQLS THTHVVDITR SSPAAKSPSA QLLEQVTQLK SLSD TIEKL KDEVLKETVS QRPGATVPTD FATFPSSAFL RAKEEQQDDT VYMGKVTFSC AAGLGQRHRL VLTQEQLHQL HDRLI S

UniProtKB: Dynactin subunit 1

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Macromolecule #11: Dynactin subunit 4

MacromoleculeName: Dynactin subunit 4 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 52.920434 KDa
SequenceString: MASLLQSERV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTAVKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPDHP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA ...String:
MASLLQSERV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTAVKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPDHP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA RRRNYMPLAF SQHTIHVVDK YGLGTRLQRP RAGTTITALA GLSLKEGEDQ KEIKIEPAQA VDEVEPLPED YY TRPVNLT EVTTLQQRLL QPDFQPICAS QLYPRHKHLL IKRSLRCRQC EHNLSKPEFN PTSIKFKIQL VAVNYIPEVR IMS IPNLRY MKESQVLLTL TNPVENLTHV TLLECEEGDP DDTNSTAKVS VPPTELVLAG KDAAAEYDEL AEPQDFPDDP DVVA FRKAN KVGVFIKVTP QREEGDVTVC FKLKHDFKNL AAPIRPVEEA DPGAEVSWLT QHVELSLGPL LP

UniProtKB: Dynactin subunit 4

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Macromolecule #12: Trafficking protein, kinesin binding 2

MacromoleculeName: Trafficking protein, kinesin binding 2 / type: protein_or_peptide / ID: 12 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 101.418789 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSQSQNAIFK SRTGEANLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ LPQYKLRVDS LFLYENQDWA QSSHQQQDAP ETLSPVLAE ETFRYMILGT DRVEQMTKTY NDIDMVTHLL AERDRDLELA ARIGQALLKR NHVLSEQNEA LEEQLGQAFD Q VNQLQHEL ...String:
MSQSQNAIFK SRTGEANLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ LPQYKLRVDS LFLYENQDWA QSSHQQQDAP ETLSPVLAE ETFRYMILGT DRVEQMTKTY NDIDMVTHLL AERDRDLELA ARIGQALLKR NHVLSEQNEA LEEQLGQAFD Q VNQLQHEL SKKDELLRIV SIASEESETD SSCSTPLRFN ESFSLSQGLL QLDMLHEKLR ELEEENMALR SKACHIKTET FT YEEKEQQ LVNDCVKELR ETNAQMSRMT EELSGKSDEL LRYQEEISSL LSQIVDLQHK LKEHVIEKEE LRLHLQASKD AQR QLTMEL HELQDRNMEC LGMLHESQEE IKELRSKSGP SAHLCFSQSY GVFTGESLAA EIEGTMRKKL SLDEESVSKQ KAQQ KRVFD TVKVANDTRG RSVTFPVLLP IPGSNRSSVI MTAKPFESGV QPAEDKTLLS PGGSTEVPGN SQPTNPPGSP EDSDL ATAL HRLSLRRQNY LSEKQFFAEE WERKIQILAE QEEEVSSCDA PTENLASVCT DQSETTDLGS ASCLRGFMPE KLQIVK PLE GSQTLHHWQQ LAQPNLGTIL DPRPGVITKG FTQVPKDVVY HISDLEEDEE EGITFQVQQP LQLEQKPALP TPVTGIF LP PMTSAGGPGT VATSNPGKCL SFTNSTFTFT TCRILHPSDI TQVTPSSGFP SLACGSSASS SSNTAVNSPA ASYRLSIG E SITNRRDSTI TFSSTRSLAK LLQERGISAK VYHSPASENP LLQPCPKALA TPSTPPNSPA QSPCSSPLPF EPRVHVSEN FLASRPAETF LQEMYGLRPS RAPPDVGQLK MNLVDRLKRL GIARVVKTPD PQENGKSREA EMGLQKPDPA VYLNSGGSLL CGLRRNQSL PVMMGSFGAP VCTTSPKMGI LKED

UniProtKB: Trafficking protein, kinesin binding 2

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Macromolecule #13: Cytoplasmic dynein 1 heavy chain 1

MacromoleculeName: Cytoplasmic dynein 1 heavy chain 1 / type: protein_or_peptide / ID: 13 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 532.739562 KDa
SequenceString: MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVG DEGEEEKEFI SYNINIDIHY GVKSNSLAFI KRAPVIDADK PVSSQLRVLT LSEDSPYETL HSFISNAVAP F FKSYIRES ...String:
MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVG DEGEEEKEFI SYNINIDIHY GVKSNSLAFI KRAPVIDADK PVSSQLRVLT LSEDSPYETL HSFISNAVAP F FKSYIRES GKADRDGDKM APSVEKKIAE LEMGLLHLQQ NIEIPEISLP IHPIITNVAK QCYERGEKPK VTDFGDKVED PT FLNQLQS GVNRWIREIQ KVTKLDRDPA SGTALQEISF WLNLERALYR IQEKRESPEV LLTLDILKHG KRFHATVSFD TDT GLKQAL ETVNDYNPLM KDFPLNDLLS ATELDKIRQA LVAIFTHLRK IRNTKYPIQR ALRLVEAISR DLSSQLLKVL GTRK LMHVA YEEFEKVMVA CFEVFQTWDD EYEKLQVLLR DIVKRKREEN LKMVWRINPA HRKLQARLDQ MRKFRRQHEQ LRAVI VRVL RPQVTAVAQQ NQGEAPEPQD MKVAEVLFDA ADANAIEEVN LAYENVKEVD GLDVSKEGTE AWEAAMKRYD ERIDRV ETR ITARLRDQLG TAKNANEMFR IFSRFNALFV RPHIRGAIRE YQTQLIQRVK DDIESLHDKF KVQYPQSQAC KMSHVRD LP PVSGSIIWAK QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFAI E STRVRGRSGN VLKLKVNFLP EIITLSKEVR NLKWLGFRVP LAIVNKAHQA NQLYPFAISL IESVRTYERT CEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV FNFQEKVDDL LIIEEKIDLE VRSLETCVYD HKTFSEILNR VQKAVDDLN LHSYSNLPIW VNKLDMEIER ILGVRLQAGL RAWTQVLLGQ AEDKAEVDMD TDAPQVSHKP GGEPKIKNVV H ELRITNQV IYLNPPIEEC RYKLYQEMFA WKMVVLSLPR IQSQRYQVGV HYELTEEEKF YRNALTRMPD GPVALEESYS AV MGIVTEV EQYVKVWLQY QCLWDMQAEN IYNRLGEDLN KWQALLVQIR KARGTFDNAE TKKEFGPVVI DYGKVQSKVN LKY DSWHKE VLSKFGQMLG SNMTEFHSQI SKSRQELEQH SVDTASTSDA VTFITYVQSL KRKIKQFEKQ VELYRNGQRL LEKQ RFQFP PSWLYIDNIE GEWGAFNDIM RRKDSAIQQQ VANLQMKIVQ EDRAVESRTT DLLADWEKTK PVTGNLRPEE ALQAL TIYE GKFGRLKDDR EKCAKAKEAL ELTETGLLSG SEERVQVALE ELQDLKGVWS ELSKIWEQID QMKEQPWVSV QPRKLR QNL DGLLNQLKNF PARLRQYASY EFVQRLLKGY LKINMLVIEL KSEALKDRHW KQLMKRLHVN WVVSELTLGQ IWDVDLQ KN EAVVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN SVSAMKLSPY YKVFEEDA L SWEDKLNRIM ALFDVWIDVQ RRWVYLEGIF TGSADIKHLL PVETQRFQSI STEFLALMKK VSKSPLVMDV LNIQGVQRS LERLADLLGK IQKALGEYLE RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILSEDN SVVLGISSRE GEEVTFKTP VSITEHPKIN EWLTLVEKEM RVTLAKLLAE SVTEVEIFGK ATSIDPNTYI TWIDKYQAQL VVLSAQIAWS E NVEAALSS IGGSGDSAPL QSVLSNVEVT LNVLADSVLM EQPPLRRRKL EHLITELVHQ RDVTRSLIKS KIDNAKSFEW LS QMRFYFD PKQTDVLQQL SIQMANAKFN YGFEYLGVQD KLVQTPLTDR CYLTMTQALE ARLGGSPFGP AGTGKTESVK ALG HQLGRF VLVFNCDETF DFQAMGRIFV GLCQVGAWGC FDEFNRLEER MLSAVSQQVQ CIQEALREHS SPNHDKASAP ITCE LLNKQ VKVSPDMAIF ITMNPGYAGR SNLPDNLKKL FRSLAMTKPD RQLIAQVMLY SQGFRTAEVL ANKIVPFFKL CDEQL SSQS HYDFGLRALK SVLVSAGNVK RERIQKIKRE KEERGEAVDE GEIAENLPEQ EILIQSVCET MVPKLVAEDI PLLFSL LSD VFPGVQYHRG EMTALREELK KVCQEMYLTY GDGEEVGGMW VEKVLQLYQI TQINHGLMMV GPSGSGKSMA WRVLLKA LE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLD D NKLLTLPNGE RLSLPPNVRI MFEVQDLKYA TLATVSRCGM VWFSEDVLST DMIFNNFLAR LRSIPLDEGE DEAQRRRKG KEDEGEEAAS PMLQIQRDAA TTLQPYFTPN GLVTKALEHA FKLEHIMDLT RLRCLGSLFS MLHQACRNVA QYNANHPDFP MQMEQLERY IQRYLVYAIL WSLSGDSRLK MRAELGEYIR RITTVPLPAA PNIPIIDYEV SISGEWSPWQ AKVPQIEVET H KVAAPDVV VPTLDTVRHE ALLYTWLAEH KPLVLCGPPG SGKTMTLFSA LRALPDMEVV GLNFSSATTP ELLLKTFDHY CE YRRTPNG VVLAPVQLGK WLVLFCDEIN LPDMDKYGTQ RVISFIRQMV EHGGFYRTSD QTWVKLERIQ FVGACNPPTD PGR KPLSHR FLRHVPVVYV DYPGPASLTQ IYGTFNRAML RLVPSLRTYA EPLTAAMVEF YTMSQERFTQ DTQPHYIYSP REMT RWVRG IFEALRPLET LPVEGLIRIW AHEALRLFQD RLVEDEERRW TDENIDLVAL KHFPNIDKEK AMSRPILYSN WLSKD YIPV DQEELRDYVK ARLKVFYEEE LDVPLVLFNE VLDHVLRIDR IFRQPQGHLL LIGVSGAGKT TLSRFVAWMN GLSVYQ IKV HRKYTGEDFD EDLRTVLRRS GCKNEKIAFI MDESNVLDSG FLERMNTLLA NGEVPGLFEG DEYATLMTQC KEGAQKE GL MLDSHEELYK WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNY V VPDYMPVVYD KLPQPPSHRE AIVNSCVFVH QTLHQANARL AKRGGRTMAI TPRHYLDFIN HYANLFHEKR SELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAV IEAQNAVKSI KKQHLVEVRS MANPPAAVKL ALESICLLLG ESTTDWKQIR SIIMRENFIP TIVNFSAEEI S DAIREKMK KNYMSNPSYN YEIVNRASLA CGPMVKWAIA QLNYADMLKR VEPLRNELQK LEDDAKDNQQ KANEVEQMIR DL EASIARY KEEYAVLISE AQAIKADLAA VEAKVNRSTA LLKSLSAERE RWEKTSETFK NQMSTIAGDC LLSAAFIAYA GYF DQQMRQ NLFTTWSHHL QQANIQFRTD IARTEYLSNA DERLRWQASS LPADDLCTEN AIMLKRFNRY PLIIDPSGQA TEFI MNEYK DRKITRTSFL DDAFRKNLES ALRFGNPLLV QDVESYDPVL NPVLNREVRR TGGRVLITLG DQDIDLSPSF VIFLS TRDP TVEFPPDLCS RVTFVNFTVT RSSLQSQCLN EVLKAERPDV DEKRSDLLKL QGEFQLRLRQ LEKSLLQALN EVKGRI LDD DTIITTLENL KREAAEVTRK VEETDIVMQE VETVSQQYLP LSTACSSIYF TMESLKQIHF LYQYSLQFFL DIYHNVL YE NPNLKGVTDH TQRLCIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYE AEFQHFLRGK EIVLSAGS T PKIPGLTVEQ AEAVVRLSCL PAFKDLIAKV QADEQFSIWL DSSSPEQTVP HLWSEENPAT PIGQAIHRLL LIQAFRPDR LLAMAHVFVS TNLGESFMSI MEQPLDLTHI VDTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA DKAINTAVK SGRWVMLKNV HLAPGWLMQL EKKLHSLQPH ACFRLFLTME INPKVPVNLL RAGRIFVFEP PPGVKANMLR T FSSVPVSR ICKSPNERAR LYFLLAWFHA IIQERLRYAP LGWSKKYEFG ESDLRSACDT VDTWLDDTAK GRQNISPDKI PW SALKTLM AQSIYGGRVD NEFDQRLLNT FLERLFTTRS FDSEFKLACK VDGHKDIQMP DGIRREEFVQ WVELLPDTQT PSW LGLPNN AERVLLTTQG VDMISKMLKM QMLEDEDDLA YAETEKKTRT DSTADGRPAW MRTLHTTASN WLHLIPQTLS HLKR TVDNI KDPLFRFFER EVKMGARLLQ DVRQDLADVV QVCEGKKKQT NYLRTLINEL VKGILPRSWS HYTVPAGMTV IQWVS DFSE RIKQLQSVSQ AAASGGAKEL KNIHVCLGGL FVPEAYITAT RQYVAQANSW SLEELCLEVI VTTSQSATLD ACSFGV TGL KLQGATCSNN KLSLSNAIST VLPLTQLRWV KQTNAEKKAN VVTLPVYLNF TRADLIFTVD FEIATKEDPR SFYERGV AV LCTE

UniProtKB: Cytoplasmic dynein 1 heavy chain 1

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Macromolecule #14: Cytoplasmic dynein 1 intermediate chain 2

MacromoleculeName: Cytoplasmic dynein 1 intermediate chain 2 / type: protein_or_peptide / ID: 14 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 68.567219 KDa
SequenceString: MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVTSVQEE SDLEKKRREA EALLQSMGLT PESPIVPPPM SPSSKSVST PSEAGSQDSG DGAVGSRRGP IKLGMAKITQ VDFPPREIVT YTKETQTPVM AQPKEDEEEE DDVVTPKPPI E PEEEKTLK ...String:
MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVTSVQEE SDLEKKRREA EALLQSMGLT PESPIVPPPM SPSSKSVST PSEAGSQDSG DGAVGSRRGP IKLGMAKITQ VDFPPREIVT YTKETQTPVM AQPKEDEEEE DDVVTPKPPI E PEEEKTLK KDEESDSKAP PHELTEEEKQ QILHSEEFLS FFDHSTRIVE RALSEQINIF FDYSGRDLED KEGEIQAGAK LS LNRQFFD ERWSKHRVVS CLDWSSQYPE LLVASYNNNE DAPHEPDGVA LVWNMKYKKT TPEYVFHCQS AVMSATFAKF HPN LVVGGT YSGQIVLWDN RSNKRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLISIS TDGKICSWSL DMLSHPQDSM ELVH KQSKA VAVTSMSFPV GDVNNFVVGS EEGSVYTACR HGSKAGISEM FEGHQGPITG IHCHAAVGAV DFSHLFVTSS FDWTV KLWT TKNNKPLYSF EDNSDYVYDV MWSPTHPALF ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIA VGD SEGQIVIYDV GEQIAVPRND EWARFGRTLA EINANRADAE EEAATRIPA

UniProtKB: Cytoplasmic dynein 1 intermediate chain 2

+
Macromolecule #15: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 15 / Number of copies: 9 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

+
Macromolecule #16: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 16 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #17: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 17 / Number of copies: 3 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated defocus max: 3.0 µm / Calibrated defocus min: 1.2 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.2 µm

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 8.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 52920
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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