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- EMDB-52524: Ku70/80 bound to WRN-exo -

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Basic information

Entry
Database: EMDB / ID: EMD-52524
TitleKu70/80 bound to WRN-exo
Map data
Sample
  • Complex: Ku70/80 bound to WRN exo and DNA
    • Protein or peptide: X-ray repair cross-complementing protein 6
    • Protein or peptide: Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
    • Protein or peptide: X-ray repair cross-complementing protein 5
    • DNA: DNA
    • DNA: DNA
  • Ligand: INOSITOL HEXAKISPHOSPHATE
  • Ligand: MAGNESIUM ION
KeywordsWRN / Ku70 / Ku80 / NHEJ / DNA BINDING PROTEIN
Function / homology
Function and homology information


3'-flap-structured DNA binding / positive regulation of strand invasion / forked DNA-dependent helicase activity / telomeric G-quadruplex DNA binding / 8-hydroxy-2'-deoxyguanosine DNA binding / telomeric D-loop binding / Ku70:Ku80 complex / DNA geometric change / negative regulation of t-circle formation / DNA end binding ...3'-flap-structured DNA binding / positive regulation of strand invasion / forked DNA-dependent helicase activity / telomeric G-quadruplex DNA binding / 8-hydroxy-2'-deoxyguanosine DNA binding / telomeric D-loop binding / Ku70:Ku80 complex / DNA geometric change / negative regulation of t-circle formation / DNA end binding / small-subunit processome assembly / telomere maintenance via semi-conservative replication / Y-form DNA binding / positive regulation of lymphocyte differentiation / telomeric D-loop disassembly / DNA-dependent protein kinase-DNA ligase 4 complex / nonhomologous end joining complex / cellular response to X-ray / four-way junction helicase activity / t-circle formation / G-quadruplex DNA binding / regulation of smooth muscle cell proliferation / bubble DNA binding / MutLalpha complex binding / double-strand break repair via classical nonhomologous end joining / Cytosolic sensors of pathogen-associated DNA / nuclear telomere cap complex / Impaired BRCA2 binding to PALB2 / protein localization to nucleolus / IRF3-mediated induction of type I IFN / response to UV-C / cellular hyperosmotic salinity response / Processive synthesis on the C-strand of the telomere / U3 snoRNA binding / Removal of the Flap Intermediate from the C-strand / regulation of telomere maintenance / recombinational repair / exonuclease activity / protein localization to chromosome, telomeric region / DNA metabolic process / 2-LTR circle formation / HDR through Single Strand Annealing (SSA) / DNA synthesis involved in DNA repair / telomeric repeat DNA binding / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / Impaired BRCA2 binding to RAD51 / DNA 3'-5' helicase / 5'-deoxyribose-5-phosphate lyase activity / 3'-5' DNA helicase activity / Presynaptic phase of homologous DNA pairing and strand exchange / ATP-dependent activity, acting on DNA / telomere maintenance via telomerase / mismatch repair / SUMOylation of DNA damage response and repair proteins / four-way junction DNA binding / 3'-5' exonuclease activity / activation of innate immune response / replication fork / telomere maintenance / cyclin binding / replication fork processing / DNA helicase activity / cellular response to starvation / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / site of DNA damage / cellular response to gamma radiation / small-subunit processome / Nonhomologous End-Joining (NHEJ) / protein-DNA complex / base-excision repair / cellular senescence / double-strand break repair via homologous recombination / G2/M DNA damage checkpoint / double-strand break repair via nonhomologous end joining / HDR through Homologous Recombination (HRR) / enzyme activator activity / double-strand break repair / manganese ion binding / transcription regulator complex / chromosome / Processing of DNA double-strand break ends / scaffold protein binding / double-stranded DNA binding / DNA recombination / secretory granule lumen / Regulation of TP53 Activity through Phosphorylation / ficolin-1-rich granule lumen / damaged DNA binding / Hydrolases; Acting on ester bonds / DNA replication / chromosome, telomeric region / nuclear speck / transcription cis-regulatory region binding / ribonucleoprotein complex
Similarity search - Function
Helicase Helix-turn-helix domain / Helix-turn-helix domain / RQC domain / RQC / RQC domain / Ku70, bridge and pillars domain superfamily / : / Ku70 / Ku, C-terminal / Ku, C-terminal domain superfamily ...Helicase Helix-turn-helix domain / Helix-turn-helix domain / RQC domain / RQC / RQC domain / Ku70, bridge and pillars domain superfamily / : / Ku70 / Ku, C-terminal / Ku, C-terminal domain superfamily / Ku C terminal domain like / Ku80 / Ku70/Ku80 C-terminal arm / Ku70/Ku80 C-terminal arm / Ku70/Ku80, N-terminal alpha/beta / Ku70/Ku80 N-terminal alpha/beta domain / Helicase and RNase D C-terminal / ATP-dependent DNA helicase RecQ, zinc-binding domain / RecQ zinc-binding / HRDC domain / HRDC domain / DNA helicase, ATP-dependent, RecQ type / HRDC domain profile. / Ku70/Ku80 beta-barrel domain / Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen / Ku70/Ku80 beta-barrel domain / SPOC-like, C-terminal domain superfamily / SAP domain superfamily / HRDC domain superfamily / 3'-5' exonuclease / SAP motif profile. / SAP domain / Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation / SAP domain / 3'-5' exonuclease / 3'-5' exonuclease domain / HRDC-like superfamily / von Willebrand factor (vWF) type A domain / von Willebrand factor, type A / DEAD/DEAH box helicase domain / DEAD/DEAH box helicase / von Willebrand factor A-like domain superfamily / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
DNA repair protein Ku70 / DNA repair protein Ku80 / Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.33 Å
AuthorsHardwick SW / Zahid S / Chaplin AK / Ropars R / Charbonnier JB
Funding support France, 1 items
OrganizationGrant numberCountry
Agence Nationale de la Recherche (ANR)ANR-20-CE11-0026 France
CitationJournal: Nat Commun / Year: 2026
Title: Structural basis of Ku-mediated activation of WRN exonuclease activity.
Authors: Sayma Zahid / Jeanne Chauvat / Ilaria Ceppi / Floriana Cappiello / Benedetta Perdichizzi / Philippe Frit / Dennis Gomez / Steven W Hardwick / Pierre Legrand / Julien Karazi / Sonia Baconnais ...Authors: Sayma Zahid / Jeanne Chauvat / Ilaria Ceppi / Floriana Cappiello / Benedetta Perdichizzi / Philippe Frit / Dennis Gomez / Steven W Hardwick / Pierre Legrand / Julien Karazi / Sonia Baconnais / Gérard Pehau-Arnaudet / Sébastien Britton / Jean-Baptiste Charbonnier / Amanda K Chaplin / Pietro Pichierri / Petr Cejka / Patrick Calsou / Virginie Ropars /
Abstract: Werner (WRN) is the only human RecQ helicase family member with DNA exonuclease activity. WRN promotes genome stability through its functions in DNA replication, repair and telomere maintenance, the ...Werner (WRN) is the only human RecQ helicase family member with DNA exonuclease activity. WRN promotes genome stability through its functions in DNA replication, repair and telomere maintenance, the deficiency of which presents clinically as Werner syndrome, causing premature aging and cancer predisposition. The main DNA double strand-break sensor Ku70/80 heterodimer (Ku) is a known partner of WRN, which stimulates its nuclease activity. However, the molecular basis of Ku-WRN interplay is currently unknown. Here, we present a high resolution cryo-EM structure of human Ku bound to DNA in complex with the N-terminal WRN exonuclease domain. This structure reveals multiple interaction sites between WRN and the Ku:DNA complex. The catalytic domain of WRN-exo engages with the DNA ends, stabilized by the vWA-like Ku80 domain interacting with the N-terminal APLF-like Ku binding motif (A-KBM) of WRN. Most surprisingly, we visualize the SAP domain of Ku70 stabilized within this complex, and we identify specific contacts mediating this interaction. These interactions are validated by assessing the impact of point mutations on either side of the Ku-WRN interfaces on exonuclease activity with purified recombinant proteins, and on live protein recruitment at biphoton laser-damaged nuclear sites. Finally, we show that disruption of WRN-Ku70 interaction results in aberrant resection of stalled replication forks. Together, we define the architecture of the Ku-WRN exonuclease domain interface and its impact on WRN exonuclease activity, recruitment and replication fork processing.
History
DepositionJan 13, 2025-
Header (metadata) releaseMay 20, 2026-
Map releaseMay 20, 2026-
UpdateJul 29, 2026-
Current statusJul 29, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52524.png

Downloads & links

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Map

FileDownload / File: emd_52524.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesX (Sec.)Y (Row.)Z (Col.)
0.65 Å/pix.
x 400 pix.
= 260.8 Å		0.65 Å/pix.
x 400 pix.
= 260.8 Å		0.65 Å/pix.
x 400 pix.
= 260.8 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.652 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0397
Minimum - Maximum-0.19517337 - 0.34389514
Average (Standard dev.)0.0002112091 (±0.009546197)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 260.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_52524_msk_1.map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_52524_half_map_1.map
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Half map: #1

Fileemd_52524_half_map_2.map
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Sample components

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Entire : Ku70/80 bound to WRN exo and DNA

EntireName: Ku70/80 bound to WRN exo and DNA
Components
  • Complex: Ku70/80 bound to WRN exo and DNA
    • Protein or peptide: X-ray repair cross-complementing protein 6
    • Protein or peptide: Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
    • Protein or peptide: X-ray repair cross-complementing protein 5
    • DNA: DNA
    • DNA: DNA
  • Ligand: INOSITOL HEXAKISPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Ku70/80 bound to WRN exo and DNA

SupramoleculeName: Ku70/80 bound to WRN exo and DNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 250 KDa

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Macromolecule #1: X-ray repair cross-complementing protein 6

MacromoleculeName: X-ray repair cross-complementing protein 6 / type: protein_or_peptide / ID: 1 / 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: Homo sapiens (human)
Molecular weightTheoretical: 69.945039 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE SQSEDELTPF DMSIQCIQSV YISKIISSDR DLLAVVFYG TEKDKNSVNF KNIYVLQELD NPGAKRILEL DQFKGQQGQK RFQDMMGHGS DYSLSEVLWV CANLFSDVQF K MSHKRIML ...String:
MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE SQSEDELTPF DMSIQCIQSV YISKIISSDR DLLAVVFYG TEKDKNSVNF KNIYVLQELD NPGAKRILEL DQFKGQQGQK RFQDMMGHGS DYSLSEVLWV CANLFSDVQF K MSHKRIML FTNEDNPHGN DSAKASRART KAGDLRDTGI FLDLMHLKKP GGFDISLFYR DIISIAEDED LRVHFEESSK LE DLLRKVR AKETRKRALS RLKLKLNKDI VISVGIYNLV QKALKPPPIK LYRETNEPVK TKTRTFNTST GGLLLPSDTK RSQ IYGSRQ IILEKEETEE LKRFDDPGLM LMGFKPLVLL KKHHYLRPSL FVYPEESLVI GSSTLFSALL IKCLEKEVAA LCRY TPRRN IPPYFVALVP QEEELDDQKI QVTPPGFQLV FLPFADDKRK MPFTEKIMAT PEQVGKMKAI VEKLRFTYRS DSFEN PVLQ QHFRNLEALA LDLMEPEQAV DLTLPKVEAM NKRLGSLVDE FKELVYPPDY NPEGKVTKRK HDNEGSGSKR PKVEYS EEE LKTHISKGTL GKFTVPMLKE ACRAYGLKSG LKKQELLEAL TKHFQD

UniProtKB: DNA repair protein Ku70

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Macromolecule #2: Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN

MacromoleculeName: Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: Hydrolases; Acting on ester bonds
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 162.677281 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MSEKKLETTA QQRKCPEWMN VQNKRCAVEE RKACVRKSVF EDDLPFLEFT GSIVYSYDAS DCSFLSEDIS MSLSDGDVVG FDMEWPPLY NRGKLGKVAL IQLCVSESKC YLFHVSSMSV FPQGLKMLLE NKAVKKAGVG IEGDQWKLLR DFDIKLKNFV E LTDVANKK ...String:
MSEKKLETTA QQRKCPEWMN VQNKRCAVEE RKACVRKSVF EDDLPFLEFT GSIVYSYDAS DCSFLSEDIS MSLSDGDVVG FDMEWPPLY NRGKLGKVAL IQLCVSESKC YLFHVSSMSV FPQGLKMLLE NKAVKKAGVG IEGDQWKLLR DFDIKLKNFV E LTDVANKK LKCTETWSLN SLVKHLLGKQ LLKDKSIRCS NWSKFPLTED QKLYAATDAY AGFIIYRNLE ILDDTVQRFA IN KEEEILL SDMNKQLTSI SEEVMDLAKH LPHAFSKLEN PRRVSILLKD ISENLYSLRR MIIGSTNIET ELRPSNNLNL LSF EDSTTG GVQQKQIREH EVLIHVEDET WDPTLDHLAK HDGEDVLGNK VERKEDGFED GVEDNKLKEN MERACLMSLD ITEH ELQIL EQQSQEEYLS DIAYKSTEHL SPNDNENDTS YVIESDEDLE MEMLKHLSPN DNENDTSYVI ESDEDLEMEM LKSLE NLNS GTVEPTHSKC LKMERNLGLP TKEEEEDDEN EANEGEEDDD KDFLWPAPNE EQVTCLKMYF GHSSFKPVQW KVIHSV LEE RRDNVAVMAT GYGKSLCFQY PPVYVGKIGL VISPLISLME DQVLQLKMSN IPACFLGSAQ SENVLTDIKL GKYRIVY VT PEYCSGNMGL LQQLEADIGI TLIAVDEAHC ISEWGHDFRD SFRKLGSLKT ALPMVPIVAL TATASSSIRE DIVRCLNL R NPQITCTGFD RPNLYLEVRR KTGNILQDLQ PFLVKTSSHW EFEGPTIIYC PSRKMTQQVT GELRKLNLSC GTYHAGMSF STRKDIHHRF VRDEIQCVIA TIAFGMGINK ADIRQVIHYG APKDMESYYQ EIGRAGRDGL QSSCHVLWAP ADINLNRHLL TEIRNEKFR LYKLKMMAKM EKYLHSSRCR RQIILSHFED KQVQKASLGI MGTEKCCDNC RSRLDHCYSM DDSEDTSWDF G PQAFKLLS AVDILGEKFG IGLPILFLRG SNSQRLADQY RRHSLFGTGK DQTESWWKAF SRQLITEGFL VEVSRYNKFM KI CALTKKG RNWLHKANTE SQSLILQANE ELCPKKLLLP SSKTVSSGTK EHCYNQVPVE LSTEKKSNLE KLYSYKPCDK ISS GSNISK KSIMVQSPEK AYSSSQPVIS AQEQETQIVL YGKLVEARQK HANKMDVPPA ILATNKILVD MAKMRPTTVE NVKR IDGVS EGKAAMLAPL LEVIKHFCQT NSVQTDLFSS TKPQEEQKTS LVAKNKICTL SQSMAITYSL FQEKKMPLKS IAESR ILPL MTIGMHLSQA VKAGCPLDLE RAGLTPEVQK IIADVIRNPP VNSDMSKISL IRMLVPENID TYLIHMAIEI LKHGPD SGL QPSCDVNKRR CFPGSEEICS SSKRSKEEVG INTETSSAER KRRLPVWFAK GSDTSKKLMD KTKRGGLFS

UniProtKB: Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN

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Macromolecule #3: X-ray repair cross-complementing protein 5

MacromoleculeName: X-ray repair cross-complementing protein 5 / type: protein_or_peptide / ID: 3 / 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: Homo sapiens (human)
Molecular weightTheoretical: 82.812438 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN KDEIALVLFG TDGTDNPLSG GDQYQNITVH RHLMLPDFD LLEDIESKIQ PGSQQADFLD ALIVSMDVIQ HETIGKKFEK RHIEIFTDLS SRFSKSQLDI IIHSLKKCDI S LQFFLPFS ...String:
MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN KDEIALVLFG TDGTDNPLSG GDQYQNITVH RHLMLPDFD LLEDIESKIQ PGSQQADFLD ALIVSMDVIQ HETIGKKFEK RHIEIFTDLS SRFSKSQLDI IIHSLKKCDI S LQFFLPFS LGKEDGSGDR GDGPFRLGGH GPSFPLKGIT EQQKEGLEIV KMVMISLEGE DGLDEIYSFS ESLRKLCVFK KI ERHSIHW PCRLTIGSNL SIRIAAYKSI LQERVKKTWT VVDAKTLKKE DIQKETVYCL NDDDETEVLK EDIIQGFRYG SDI VPFSKV DEEQMKYKSE GKCFSVLGFC KSSQVQRRFF MGNQVLKVFA ARDDEAAAVA LSSLIHALDD LDMVAIVRYA YDKR ANPQV GVAFPHIKHN YECLVYVQLP FMEDLRQYMF SSLKNSKKYA PTEAQLNAVD ALIDSMSLAK KDEKTDTLED LFPTT KIPN PRFQRLFQCL LHRALHPREP LPPIQQHIWN MLNPPAEVTT KSQIPLSKIK TLFPLIEAKK KDQVTAQEIF QDNHED GPT AKKLKTEQGG AHFSVSSLAE GSVTSVGSVN PAENFRVLVK QKKASFEEAS NQLINHIEQF LDTNETPYFM KSIDCIR AF REEAIKFSEE QRFNNFLKAL QEKVEIKQLN HFWEIVVQDG ITLITKEEAS GSSVTAEEAK KFLAPKDKPS GDTAAVFE E GGDVDDLLDM I

UniProtKB: DNA repair protein Ku80

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Macromolecule #4: DNA

MacromoleculeName: DNA / type: dna / ID: 4 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 5.253415 KDa
SequenceString:
(DT)(DT)(DT)(DT)(DA)(DG)(DT)(DT)(DT)(DA) (DT)(DT)(DG)(DG)(DG)(DT)(DA)

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Macromolecule #5: DNA

MacromoleculeName: DNA / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 5.195453 KDa
SequenceString:
(DA)(DT)(DC)(DT)(DA)(DA)(DT)(DA)(DA)(DA) (DC)(DT)(DA)(DA)(DA)(DA)(DA)

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Macromolecule #6: INOSITOL HEXAKISPHOSPHATE

MacromoleculeName: INOSITOL HEXAKISPHOSPHATE / type: ligand / ID: 6 / Number of copies: 1 / Formula: IHP
Molecular weightTheoretical: 660.035 Da
Chemical component information

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

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Macromolecule #7: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 7 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration3 mg/mL
BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Average electron dose: 47.24 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.7000000000000001 µm / Nominal magnification: 130000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 262908
CTF correctionSoftware - Name: Warp / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.33 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 83379
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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