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- EMDB-76020: Cryo-EM structure of DNA polymerase Zeta with RNA:DNA hybrid and ... -

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Basic information

Entry
Database: EMDB / ID: EMD-76020
TitleCryo-EM structure of DNA polymerase Zeta with RNA:DNA hybrid and incoming dNTP
Map data
Sample
  • Complex: protein complex
    • Complex: protein complex
      • Protein or peptide: x 5 types
    • Complex: nucleic acid
      • DNA: x 1 types
      • RNA: x 1 types
  • Ligand: x 4 types
KeywordsProtein complex / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA-RNA complex
Function / homology
Function and homology information


Translesion synthesis by REV1 / delta DNA polymerase complex / DNA amplification / deoxycytidyl transferase activity / H3-H4 histone complex chaperone activity / zeta DNA polymerase complex / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / RNA-templated DNA biosynthetic process / DNA replication, removal of RNA primer ...Translesion synthesis by REV1 / delta DNA polymerase complex / DNA amplification / deoxycytidyl transferase activity / H3-H4 histone complex chaperone activity / zeta DNA polymerase complex / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / RNA-templated DNA biosynthetic process / DNA replication, removal of RNA primer / lagging strand elongation / DNA damage tolerance / error-free translesion synthesis / double-strand break repair via break-induced replication / DNA metabolic process / DNA strand elongation involved in DNA replication / leading strand elongation / error-prone translesion synthesis / mismatch repair / translesion synthesis / replication fork / double-strand break repair via homologous recombination / nucleotide-excision repair / base-excision repair / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / site of double-strand break / DNA-directed DNA polymerase / damaged DNA binding / DNA-directed DNA polymerase activity / molecular adaptor activity / nucleotide binding / DNA repair / chromatin / mitochondrion / DNA binding / nucleus / cytosol / cytoplasm
Similarity search - Function
DNA polymerase delta subunit, OB-fold domain / DNA polymerase delta subunit 2, C-terminal domain / DNA polymerase delta subunit OB-fold domain / DNA polymerase zeta catalytic subunit / : / DNA polymerase zeta catalytic subunit, N-terminal / DNA repair protein Rev1 / DNA polymerase delta/II small subunit family / C4-type zinc-finger of DNA polymerase delta / : ...DNA polymerase delta subunit, OB-fold domain / DNA polymerase delta subunit 2, C-terminal domain / DNA polymerase delta subunit OB-fold domain / DNA polymerase zeta catalytic subunit / : / DNA polymerase zeta catalytic subunit, N-terminal / DNA repair protein Rev1 / DNA polymerase delta/II small subunit family / C4-type zinc-finger of DNA polymerase delta / : / C4-type zinc-finger of DNA polymerase delta / DNA polymerase delta catalytic subunit-like, N-terminal domain / Mad2-like / HORMA domain / HORMA domain / HORMA domain profile. / HORMA domain superfamily / : / DNA polymerase-iota, thumb domain / DNA polymerase alpha/delta/epsilon, subunit B / DNA polymerase alpha/epsilon subunit B / Ubiquitin-binding motif (UBM) domain profile. / BRCT domain / DNA polymerase family B, thumb domain / DNA-directed DNA polymerase, family B, multifunctional domain / DNA-directed DNA polymerase, family B, conserved site / DNA polymerase family B signature. / DNA polymerase family B / DNA polymerase, Y-family, little finger domain / impB/mucB/samB family C-terminal domain / UmuC domain / DNA polymerase, Y-family, little finger domain superfamily / impB/mucB/samB family / UmuC domain profile. / DNA polymerase family B, exonuclease domain / DNA-directed DNA polymerase, family B, exonuclease domain / DNA polymerase, palm domain superfamily / DNA polymerase type-B family / DNA-directed DNA polymerase, family B / breast cancer carboxy-terminal domain / BRCT domain profile. / BRCT domain / BRCT domain superfamily / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
Translesion synthesis protein REV1 / DNA polymerase zeta catalytic subunit / DNA polymerase zeta processivity subunit / DNA polymerase delta small subunit / DNA polymerase delta subunit 3
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.03 Å
AuthorsMalik R / Aggarwal AK
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI) United States
CitationJournal: Nat Commun / Year: 2026
Title: Molecular basis of DNA polymerase zeta's reverse transcriptase activity
Authors: Malik R / Johnson RE / Prakash L / Prakash S / Aggarwal AK
History
DepositionMar 11, 2026-
Header (metadata) releaseOct 7, 2026-
Map releaseOct 7, 2026-
UpdateOct 7, 2026-
Current statusOct 7, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_76020.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 320 pix.
= 264.32 Å
0.83 Å/pix.
x 320 pix.
= 264.32 Å
0.83 Å/pix.
x 320 pix.
= 264.32 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.826 Å
Density
Contour LevelBy AUTHOR: 0.28
Minimum - Maximum-1.2825576 - 3.5522575
Average (Standard dev.)0.004771772 (±0.07920992)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 264.32 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_76020_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_76020_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : protein complex

EntireName: protein complex
Components
  • Complex: protein complex
    • Complex: protein complex
      • Protein or peptide: DNA polymerase zeta catalytic subunit
      • Protein or peptide: DNA polymerase zeta processivity subunit
      • Protein or peptide: DNA polymerase delta subunit 3
      • Protein or peptide: DNA repair protein REV1
      • Protein or peptide: DNA polymerase delta small subunit
    • Complex: nucleic acid
      • DNA: DNA (5'-D(P*AP*TP*TP*AP*CP*GP*AP*AP*TP*TP*GP*C)-3')
      • RNA: RNA (5'-R(P*AP*AP*UP*GP*GP*CP*AP*AP*UP*UP*CP*GP*UP*AP*AP*U)-3')
  • Ligand: CALCIUM ION
  • Ligand: 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
  • Ligand: IRON/SULFUR CLUSTER
  • Ligand: water

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Supramolecule #1: protein complex

SupramoleculeName: protein complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7

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Supramolecule #2: protein complex

SupramoleculeName: protein complex / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#4, #6
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #3: nucleic acid

SupramoleculeName: nucleic acid / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #5, #7
Source (natural)Organism: synthetic construct (others) / Synthetically produced: Yes

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Macromolecule #1: DNA polymerase zeta catalytic subunit

MacromoleculeName: DNA polymerase zeta catalytic subunit / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed DNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 177.068516 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MDYKDDDDKG DHNHRHKHGD PLEVLFQGPG GDPHMSRESN DTIQSDTVRS SSKSDYFRIQ LNNQDYYMSK PTFLDPSHGE SLPLNQFSQ VPNIRVFGAL PTGHQVLCHV HGILPYMFIK YDGQITDTST LRHQRCAQVH KTLEVKIRAS FKRKKDDKHD L AGDKLGNL ...String:
MDYKDDDDKG DHNHRHKHGD PLEVLFQGPG GDPHMSRESN DTIQSDTVRS SSKSDYFRIQ LNNQDYYMSK PTFLDPSHGE SLPLNQFSQ VPNIRVFGAL PTGHQVLCHV HGILPYMFIK YDGQITDTST LRHQRCAQVH KTLEVKIRAS FKRKKDDKHD L AGDKLGNL NFVADVSVVK GIPFYGYHVG WNLFYKISLL NPSCLSRISE LIRDGKIFGK KFEIYESHIP YLLQWTADFN LF GCSWINV DRCYFRSPVL NSILDIDKLT INDDLQLLLD RFCDFKCNVL SRRDFPRVGN GLIEIDILPQ FIKNREKLQH RDI HHDFLE KLGDISDIPV KPYVSSARDM INELTMQREE LSLKEYKEPP ETKRHVSGHQ WQSSGEFEAF YKKAQHKTST FDGQ IPNFE NFIDKNQKFS AINTPYEALP QLWPRLPQIE INNNSMQDKK NDDQVNASFT EYEICGVDNE NEGVKGSNIK SRSYS WLPE SIASPKDSTI LLDHQTKYHN TINFSMDCAM TQNMASKRKL RSSVSANKTS LLSRKRKKVM AAGLRYGKRA FVYGEP PFG YQDILNKLED EGFPKIDYKD PFFSNPVDLE NKPYAYAGKR FEISSTHVST RIPVQFGGET VSVYNKPTFD MFSSWKY AL KPPTYDAVQK WYNKVPSMGN KKTESQISMH TPHSKFLYKF ASDVSGKQKR KKSSVHDSLT HLTLEIHANT RSDKIPDP A IDEVSMIIWC LEEETFPLDL DIAYEGIMIV HKASEDSTFP TKIQHCINEI PVMFYESEFE MFEALTDLVL LLDPDILSG FEIHNFSWGY IIERCQKIHQ FDIVRELARV KCQIKTKLSD TWGYAHSSGI MITGRHMINI WRALRSDVNL TQYTIESAAF NILHKRLPH FSFESLTNMW NAKKSTTELK TVLNYWLSRA QINIQLLRKQ DYIARNIEQA RLIGIDFHSV YYRGSQFKVE S FLIRICKS ESFILLSPGK KDVRKQKALE CVPLVMEPES AFYKSPLIVL DFQSLYPSIM IGYNYCYSTM IGRVREINLT EN NLGVSKF SLPRNILALL KNDVTIAPNG VVYAKTSVRK STLSKMLTDI LDVRVMIKKT MNEIGDDNTT LKRLLNNKQL ALK LLANVT YGYTSASFSG RMPCSDLADS IVQTGRETLE KAIDIIEKDE TWNAKVVYGD TDSLFVYLPG KTAIEAFSIG HAMA ERVTQ NNPKPIFLKF EKVYHPSILI SKKRYVGFSY ESPSQTLPIF DAKGIETVRR DGIPAQQKII EKCIRLLFQT KDLSK IKKY LQNEFFKIQI GKVSAQDFCF AKEVKLGAYK SEKTAPAGAV VVKRRINEDH RAEPQYKERI PYLVVKGKQG QLLRER CVS PEEFLEGENL ELDSEYYINK ILIPPLDRLF NLIGINVGNW AQEIVKSKRA STTTTKVENI TRVGTSATCC NCGEELT KI CSLQLCDDCL EKRSTTTLSF LIKKLKRQKE YQTLKTVCRT CSYRYTSDAG IENDHIASKC NSYDCPVFYS RVKAERYL R DNQSVQREEA LISLNDW

UniProtKB: DNA polymerase zeta catalytic subunit

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Macromolecule #2: DNA polymerase zeta processivity subunit

MacromoleculeName: DNA polymerase zeta processivity subunit / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 28.791654 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MNRWVEKWLR VYLKCYINLI LFYRNVYPPQ SFDYTTYQSF NLPQFVPINR HPALIDYIEE LILDVLSKLT HVYRFSICII NKKNDLCIE KYVLDFSELQ HVDKDDQIIT ETEVFDEFRS SLNSLIMHLE KLPKVNDDTI TFEAVINAIE LELGHKLDRN R RVDSLEEK ...String:
MNRWVEKWLR VYLKCYINLI LFYRNVYPPQ SFDYTTYQSF NLPQFVPINR HPALIDYIEE LILDVLSKLT HVYRFSICII NKKNDLCIE KYVLDFSELQ HVDKDDQIIT ETEVFDEFRS SLNSLIMHLE KLPKVNDDTI TFEAVINAIE LELGHKLDRN R RVDSLEEK AEIERDSNWV KCQEDENLPD NNGFQPPKIK LTSLVGSDVG PLIIHQFSEK LISGDDKILN GVYSQYEEGE SI FGSLF

UniProtKB: DNA polymerase zeta processivity subunit

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Macromolecule #3: DNA polymerase delta subunit 3

MacromoleculeName: DNA polymerase delta subunit 3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 40.377715 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MDQKASYFIN EKLFTEVKPV LFTDLIHHLK IGPSMAKKLM FDYYKQTTNA KYNCVVICCY KDQTIKIIHD LSNIPQQDSI IDCFIYAFN PMDSFIPYYD IIDQKDCLTI KNSYELKVSE SSKIIERTKT LEEKSKPLVR PTARSKTTPE ETTGRKSKSK D MGLRSTAL ...String:
MDQKASYFIN EKLFTEVKPV LFTDLIHHLK IGPSMAKKLM FDYYKQTTNA KYNCVVICCY KDQTIKIIHD LSNIPQQDSI IDCFIYAFN PMDSFIPYYD IIDQKDCLTI KNSYELKVSE SSKIIERTKT LEEKSKPLVR PTARSKTTPE ETTGRKSKSK D MGLRSTAL LAKMKKDRDD KETSRQNELR KRKEENLQKI NKQNPEREAQ MKELNNLFVE DDLDTEEVNG GSKPNSPKET DS NDKDKNN DDLEDLLETT AEDSLMDVPK IQQTKPSETE HSKEPKSEEE PSSFIDEDGY IVTKRPATST PPRKPSPVVK RAL SSSKKQ ETPSSNKRLK KQGTLESFFK RKAK

UniProtKB: DNA polymerase delta subunit 3

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Macromolecule #4: DNA repair protein REV1

MacromoleculeName: DNA repair protein REV1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
EC number: Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 112.384219 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MGEHGGLVDL LDSDLEYSIN RETPDKNNCL SQQSVNDSHL TAKTGGLNAR SFLSTLSDDS LIEYVNQLSQ TNKNNSNPTA GTLRFTTKN ISCDELHADL GGGEDSPIAR SVIEIQESDS NGDDVKKNTV YTREAYFHEK AHGQTLQDQI LKDQYKDQIS S QSSKIFKN ...String:
MGEHGGLVDL LDSDLEYSIN RETPDKNNCL SQQSVNDSHL TAKTGGLNAR SFLSTLSDDS LIEYVNQLSQ TNKNNSNPTA GTLRFTTKN ISCDELHADL GGGEDSPIAR SVIEIQESDS NGDDVKKNTV YTREAYFHEK AHGQTLQDQI LKDQYKDQIS S QSSKIFKN CVIYINGYTK PGRLQLHEMI VLHGGKFLHY LSSKKTVTHI VASNLPLKKR IEFANYKVVS PDWIVDSVKE AR LLPWQNY SLTSKLDEQQ KKLDNCKTVN SIPLPSETSL HKGSKCVGSA LLPVEQQSPV NLNNLEAKRI VACDDPDFLT SYF AHSRLH HLSAWKANLK DKFLNENIHK YTKITDKDTY IIFHIDFDCF FATVAYLCRS SSFSACDFKR DPIVVCHGTK NSDI ASCNY VARSYGIKNG MWVSQAEKML PNGIKLISLP YTFEQFQLKS EAFYSTLKRL NIFNLILPIS IDEAVCVRII PDNIH NTNT LNARLCEEIR QEIFQGTNGC TVSIGCSDSL VLARLALKMA KPNGYNITFK SNLSEEFWSS FKLDDLPGVG HSTLSR LES TFDSPHSLND LRKRYTLDAL KASVGSKLGM KIHLALQGQD DEESLKILYD PKEVLQRKSL SIDINWGIRF KNITQVD LF IERGCQYLLE KLNEINKTTS QITLKLMRRC KDAPIEPPKY MGMGRCDSFS RSSRLGIPTN EFGIIATEMK SLYRTLGC P PMELRGLALQ FNKLVDVGPD NNQLKLRLPF KTIVTNRAFE ALPEDVKNDI NNEFEKRNYK RKESGLTSNS LSSKKKGFA ISRLEVNDLP STMEEQFMNE LPTQIRAEVR HDLRIQKKIQ QTKLGNLQEK IKRREESLQN EKNHFMGQNS IFQPIKFQNL TRFKKICQL VKQWVAETLG DGGPHEKDVK LFVKYLIKLC DSNRVHLVLH LSNLISRELN LCAFLNQDHS GFQTWERILL N DIIPLLNR NKHTYQTVRK LDMDFEV

UniProtKB: Translesion synthesis protein REV1

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Macromolecule #6: DNA polymerase delta small subunit

MacromoleculeName: DNA polymerase delta small subunit / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed DNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 55.987352 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: GPGGDLHMDA LLTKFNEDRS LQDENLSQPR TRVRIVDDNL YNKSNPFQLC YKKRDYGSQY YHIYQYRLKT FRERVLKECD KRWDAGFTL NGQLVLKKDK VLDIQGNQPC WCVGSIYCEM KYKPNVLDEV INDTYGAPDL TKSYTDKEGG SDEIMLEDES G RVLLVGDF ...String:
GPGGDLHMDA LLTKFNEDRS LQDENLSQPR TRVRIVDDNL YNKSNPFQLC YKKRDYGSQY YHIYQYRLKT FRERVLKECD KRWDAGFTL NGQLVLKKDK VLDIQGNQPC WCVGSIYCEM KYKPNVLDEV INDTYGAPDL TKSYTDKEGG SDEIMLEDES G RVLLVGDF IRSTPFITGV VVGILGMEAE AGTFQVLDIC YPTPLPQNPF PAPIATCPTR GKIALVSGLN LNNTSPDRLL RL EILREFL MGRINNKIDD ISLIGRLLIC GNSVDFDIKS VNKDELMISL TEFSKFLHNI LPSISVDIMP GTNDPSDKSL PQQ PFHKSL FDKSLESYFN GSNKEILNLV TNPYEFSYNG VDVLAVSGKN INDICKYVIP SNDNGESENK VEEGESNDFK DDIE HRLDL MECTMKWQNI APTAPDTLWC YPYTDKDPFV LDKWPHVYIV ANQPYFGTRV VEIGGKNIKI ISVPEFSSTG MIILL DLET LEAETVKIDI

UniProtKB: DNA polymerase delta small subunit

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Macromolecule #5: DNA (5'-D(P*AP*TP*TP*AP*CP*GP*AP*AP*TP*TP*GP*C)-3')

MacromoleculeName: DNA (5'-D(P*AP*TP*TP*AP*CP*GP*AP*AP*TP*TP*GP*C)-3') / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 6.132991 KDa
SequenceString:
(DT)(DG)(DA)(DC)(DC)(DA)(DT)(DG)(DA)(DT) (DT)(DA)(DC)(DG)(DA)(DA)(DT)(DT)(DG)(DC)

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Macromolecule #7: RNA (5'-R(P*AP*AP*UP*GP*GP*CP*AP*AP*UP*UP*CP*GP*UP*AP*AP*U)-3')

MacromoleculeName: RNA (5'-R(P*AP*AP*UP*GP*GP*CP*AP*AP*UP*UP*CP*GP*UP*AP*AP*U)-3')
type: rna / ID: 7 / Number of copies: 1
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 7.984772 KDa
SequenceString:
UAAUGGCAAU UCGUAAUCAU GGUCA

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Macromolecule #8: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 8 / Number of copies: 1 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #9: 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE

MacromoleculeName: 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 1 / Formula: DCP
Molecular weightTheoretical: 467.157 Da
Chemical component information

ChemComp-DCP:
2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE

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Macromolecule #10: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 10 / Number of copies: 1 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

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Macromolecule #11: water

MacromoleculeName: water / type: ligand / ID: 11 / Number of copies: 7 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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

BufferpH: 6.5
Sugar embeddingMaterial: VITREOUS ICE
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 54.24 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: 0.5 µm
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: OTHER / Details: Ab-initio model
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. v4.7) / Number images used: 544413
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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