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- EMDB-7821: CryoEM structure of Tetrahymena telomerase with telomeric DNA at ... -

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Basic information

Entry
Database: EMDB / ID: EMD-7821
TitleCryoEM structure of Tetrahymena telomerase with telomeric DNA at 4.8 Angstrom resolution
Map dataTetrahymena telomerase with telomeric DNA
Sample
  • Complex: Endogenous assembled Tetrahymena telomerase bound with telomeric DNA
    • Protein or peptide: Telomerase-associated protein 82
    • Protein or peptide: Telomerase reverse transcriptase
    • Protein or peptide: Telomerase holoenzyme TEB heterotrimer Teb3 subunit
    • Protein or peptide: Telomerase holoenzyme Teb2 subunit
    • RNA: RNA (159-MER)
    • Protein or peptide: Telomerase-associated protein 50
    • Protein or peptide: Telomerase La-related protein p65
    • DNA: DNA (5'-D(P*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP*G)-3')
  • Ligand: ZINC ION
KeywordsTelomerase / telomere / REPLICATION
Function / homology
Function and homology information


telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase catalytic core complex / DNA replication factor A complex / telomerase activity / single-stranded telomeric DNA binding / telomerase holoenzyme complex / telomerase RNA binding / telomeric DNA binding / telomere maintenance via telomerase ...telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase catalytic core complex / DNA replication factor A complex / telomerase activity / single-stranded telomeric DNA binding / telomerase holoenzyme complex / telomerase RNA binding / telomeric DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase / DNA recombination / chromosome, telomeric region / DNA replication / DNA repair / DNA binding / zinc ion binding / metal ion binding
Similarity search - Function
: / Telomerase reverse transcriptase, TEN domain / Telomerase reverse transcriptase, CTE domain / Replication factor A protein 3 / Replication factor A protein 3 / La protein, xRRM domain / xRRM domain profile. / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function ...: / Telomerase reverse transcriptase, TEN domain / Telomerase reverse transcriptase, CTE domain / Replication factor A protein 3 / Replication factor A protein 3 / La protein, xRRM domain / xRRM domain profile. / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function / La-type HTH domain / La-type HTH domain profile. / Telomerase ribonucleoprotein complex - RNA binding domain / : / Telomerase reverse transcriptase / Telomerase ribonucleoprotein complex - RNA-binding domain / Telomerase ribonucleoprotein complex - RNA binding domain / Replication factor A, C-terminal / Replication factor-A C terminal domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Reverse transcriptase domain / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase (RT) catalytic domain profile. / Winged helix DNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
Replication protein A 32 kDa subunit / Replication protein A 14 kDa subunit / Telomeric repeat-binding subunit 1 / Telomerase reverse transcriptase / La-related protein 7 homolog
Similarity search - Component
Biological speciesTetrahymena thermophila (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.8 Å
AuthorsJiang J / Wang Y / Susac L / Chan H / Basu R / Zhou ZH / Feigon J
Funding support United States, 9 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM048123 United States
National Science Foundation (NSF, United States)MCB1517625 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM071940 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM007185 United States
National Institutes of Health/Office of the Director1S10OD018111 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1U24GM116792 United States
National Science Foundation (NSF, United States)DBI-1338135 United States
National Science Foundation (NSF, United States)DMR-1548924 United States
American Heart Association14POST18870059 United States
CitationJournal: Cell / Year: 2018
Title: Structure of Telomerase with Telomeric DNA.
Authors: Jiansen Jiang / Yaqiang Wang / Lukas Sušac / Henry Chan / Ritwika Basu / Z Hong Zhou / Juli Feigon /
Abstract: Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA ...Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA (TER). Its activity is a critical determinant of human health, affecting aging, cancer, and stem cell renewal. Lack of atomic models of telomerase, particularly one with DNA bound, has limited our mechanistic understanding of telomeric DNA repeat synthesis. We report the 4.8 Å resolution cryoelectron microscopy structure of active Tetrahymena telomerase bound to telomeric DNA. The catalytic core is an intricately interlocked structure of TERT and TER, including a previously structurally uncharacterized TERT domain that interacts with the TEN domain to physically enclose TER and regulate activity. This complete structure of a telomerase catalytic core and its interactions with telomeric DNA from the template to telomere-interacting p50-TEB complex provides unanticipated insights into telomerase assembly and catalytic cycle and a new paradigm for a reverse transcriptase RNP.
History
DepositionApr 22, 2018-
Header (metadata) releaseMay 30, 2018-
Map releaseMay 30, 2018-
UpdateJul 16, 2025-
Current statusJul 16, 2025Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.055
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.055
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6d6v
  • Surface level: 0.055
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_7821.png

Downloads & links

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Map

FileDownload / File: emd_7821.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTetrahymena telomerase with telomeric DNA
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.36 Å/pix.
x 256 pix.
= 348.16 Å		1.36 Å/pix.
x 256 pix.
= 348.16 Å		1.36 Å/pix.
x 256 pix.
= 348.16 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.36 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.055 / Movie #1: 0.055
Minimum - Maximum-0.054381963 - 0.15599543
Average (Standard dev.)-0.000078641795 (±0.0058957483)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-128-128-128
Dimensions256256256
Spacing256256256
CellA=B=C: 348.16 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.361.361.36
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z348.160348.160348.160
α/β/γ90.00090.00090.000
start NX/NY/NZ-199-199-199
NX/NY/NZ399399399
MAP C/R/S123
start NC/NR/NS-128-128-128
NC/NR/NS256256256
D min/max/mean-0.0540.156-0.000

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Supplemental data

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Mask #1

Fileemd_7821_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Endogenous assembled Tetrahymena telomerase bound with telomeric DNA

EntireName: Endogenous assembled Tetrahymena telomerase bound with telomeric DNA
Components
  • Complex: Endogenous assembled Tetrahymena telomerase bound with telomeric DNA
    • Protein or peptide: Telomerase-associated protein 82
    • Protein or peptide: Telomerase reverse transcriptase
    • Protein or peptide: Telomerase holoenzyme TEB heterotrimer Teb3 subunit
    • Protein or peptide: Telomerase holoenzyme Teb2 subunit
    • RNA: RNA (159-MER)
    • Protein or peptide: Telomerase-associated protein 50
    • Protein or peptide: Telomerase La-related protein p65
    • DNA: DNA (5'-D(P*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP*G)-3')
  • Ligand: ZINC ION

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Supramolecule #1: Endogenous assembled Tetrahymena telomerase bound with telomeric DNA

SupramoleculeName: Endogenous assembled Tetrahymena telomerase bound with telomeric DNA
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Tetrahymena thermophila (eukaryote)

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Macromolecule #1: Telomerase-associated protein 82

MacromoleculeName: Telomerase-associated protein 82 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 82.040289 KDa
SequenceString: MKLTKGGSYI LKKVDRKQFY QDEEIVMQIK KILGQKTTDC KQYIKCECID GLGDEALIYF EMLANQNQHL QKNDVIMIQD YLNDKTQND KIVVLVTRFQ FCKASHVQPK TAQKESIQLL NTEKTIIQKS KITKNPAEEV LKFIEVNEKD NSSNSEDMII E QQKQEIKN ...String:
MKLTKGGSYI LKKVDRKQFY QDEEIVMQIK KILGQKTTDC KQYIKCECID GLGDEALIYF EMLANQNQHL QKNDVIMIQD YLNDKTQND KIVVLVTRFQ FCKASHVQPK TAQKESIQLL NTEKTIIQKS KITKNPAEEV LKFIEVNEKD NSSNSEDMII E QQKQEIKN NQKEKQSING FNLEDSYSNI SDITNFGGKS NFNIGSLSDQ LSKQTLLISQ LQVGKNRFSF KFEGRVVYKS ST FQNQQDS KYFFITAQDA NNQEINLSFW QKVDQSYQTL KVGQYYYFIG GEVKQFKNNL ELKFKFGDYQ IIPKETLSAN YVQ PLALQP SKQFGNDSIG DSDYSIHNLI EKEESIAQKG YNGQKNNKYR QNNNNSKHTL LISEVLKTSK QYLSVLAQVV DIQS SDKNI RLKICDNSCN QELKVVIFPD LCYEWRDKFS INKWYYFNEF VRQIYNDEVQ LKNNIHSSIK ESDDQRKVIT YNQEQ GVFK KSISINSNDS FEIKPKISYK NNSNQEQRIY SSIEEIIQQA QASEIGQKKE FYVYGNLVSI QMKNKLYYYR CTCQGK SVL KYHGDSFFCE SCQQFINPQV HLMLRAFVQD STGTIPVMIF DQQSSQLINQ IDPSIHVQEA GQYVKNCIEN GQEEIIR QL FSKLDFARFI FEIQFENKEF NNEQEIAYKV LKIEKENIKE ESKYLLKKLE HLINNNQNN

UniProtKB: Telomeric repeat-binding subunit 1

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Macromolecule #2: Telomerase reverse transcriptase

MacromoleculeName: Telomerase reverse transcriptase / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA-directed DNA polymerase
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 133.486938 KDa
SequenceString: MQKINNINNN KQMLTRKEDL LTVLKQISAL KYVSNLYEFL LATEKIVQTS ELDTQFQEFL TTTIIASEQN LVENYKQKYN QPNFSQLTI KQVIDDSIIL LGNKQNYVQQ IGTTTIGFYV EYENINLSRQ TLYSSNFRNL LNIFGEEDFK YFLIDFLVFT K VEQNGYLQ ...String:
MQKINNINNN KQMLTRKEDL LTVLKQISAL KYVSNLYEFL LATEKIVQTS ELDTQFQEFL TTTIIASEQN LVENYKQKYN QPNFSQLTI KQVIDDSIIL LGNKQNYVQQ IGTTTIGFYV EYENINLSRQ TLYSSNFRNL LNIFGEEDFK YFLIDFLVFT K VEQNGYLQ VAGVCLNQYF SVQVKQKKWY KNNFNMNGKA TSNNNQNNAN LSNEKKQENQ YIYPEIQRSQ IFYCNHMGRE PG VFKSSFF NYSEIKKGFQ FKVIQEKLQG RQFINSDKIK PDHPQTIIKK TLLKEYQSKN FSCQEERDLF LEFTEKIVQN FHN INFNYL LKKFCKLPEN YQSLKSQVKQ IVQSENKANQ QSCENLFNSL YDTEISYKQI TNFLRQIIQN CVPNQLLGKK NFKV FLEKL YEFVQMKRFE NQKVLDYICF MDVFDVEWFV DLKNQKFTQK RKYISDKRKI LGDLIVFIIN KIVIPVLRYN FYITE KHKE GSQIFYYRKP IWKLVSKLTI VKLEEENLEK VEEKLIPEDS FQKYPQGKLR IIPKKGSFRP IMTFLRKDKQ KNIKLN LNQ ILMDSQLVFR NLKDMLGQKI GYSVFDNKQI SEKFAQFIEK WKNKGRPQLY YVTLDIKKCY DSIDQMKLLN FFNQSDL IQ DTYFINKYLL FQRNKRPLLQ IQQTNNLNSA MEIEEEKINK KPFKMDNINF PYYFNLKERQ IAYSLYDDDD QILQKGFK E IQSDDRPFIV INQDKPRCIT KDIIHNHLKH ISQYNVISFN KVKFRQKRGI PQGLNISGVL CSFYFGKLEE EYTQFLKNA EQVNGSINLL MRLTDDYLFI SDSQQNALNL IVQLQNCANN NGFMFNDQKI TTNFQFPQED YNLEHFKISV QNECQWIGKS IDMNTLEIK SIQKQTQQEI NQTINVAISI KNLKSQLKNK LRSLFLNQLI DYFNPNINSF EGLCRQLYHH SKATVMKFYP F MTKLFQID LKKSKQYSVQ YGKENTNENF LKDILYYTVE DVCKILCYLQ FEDEINSNIK EIFKNLYSWI MWDIIVSYLK KK KQFKGYL NKLLQKIRKS RFFYLKEGCK SLQLILSQQK YQLNKKELEA IEFIDLNNLI QDIKTLIPKI SAKSNQQNTN

UniProtKB: Telomerase reverse transcriptase

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Macromolecule #3: Telomerase holoenzyme TEB heterotrimer Teb3 subunit

MacromoleculeName: Telomerase holoenzyme TEB heterotrimer Teb3 subunit / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 14.007626 KDa
SequenceString:
MDAEQEQVMY PRILFEQMAQ FRGKKVTVVG NVCNEDQNDS LVIEFGPTGL NQHVVIDNYR RVDLNNTTKF VEIRGVVLNQ NIVSCEELT EFEQKDPFDF DTYSKLIHLS QSDKLSSLFT DQ

UniProtKB: Replication protein A 14 kDa subunit

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Macromolecule #4: Telomerase holoenzyme Teb2 subunit

MacromoleculeName: Telomerase holoenzyme Teb2 subunit / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 30.993035 KDa
SequenceString: MSNRVQGGFD NNSGNNQSAQ KQQAEKIPQI TVPLNCFMIN QIVKAAKENP QAHSGNHYEW YGAFENAIIT AKFEFLQSIN DSPKIMGKL SDSTGCIEVV IQKSKMSDEL PEFVQAYEIE LQNNGNRHKY VRAMLKMRKN AQIQLLYFSI VNDANEISRH G LDLCLRYL ...String:
MSNRVQGGFD NNSGNNQSAQ KQQAEKIPQI TVPLNCFMIN QIVKAAKENP QAHSGNHYEW YGAFENAIIT AKFEFLQSIN DSPKIMGKL SDSTGCIEVV IQKSKMSDEL PEFVQAYEIE LQNNGNRHKY VRAMLKMRKN AQIQLLYFSI VNDANEISRH G LDLCLRYL QRKHGIEDFM HMTNDKAHNN HNASAQKVHY QIDRNQQPKE QVLELMRQIL KHNPNDQIPK SKIIEFFQSQ LN QVQINQI LQQLVSANEI FSVGSDNYLL NV

UniProtKB: Replication protein A 32 kDa subunit

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Macromolecule #6: Telomerase-associated protein 50

MacromoleculeName: Telomerase-associated protein 50 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 13.379484 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #7: Telomerase La-related protein p65

MacromoleculeName: Telomerase La-related protein p65 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 64.207363 KDa
SequenceString: MDEYLENTNL EELEQECFME DYQHEDVVEQ ENHQVDANDI YENQQMNDES QLNQDVKISQ QKEQAVEMIE EQQQNNQDKF KQFQDCMAH ITELNFKRNY QNLTEQSSSN NVVAEELDIK ESLKLQMEYY FCDTNLTHDS YLRGIISKSP KNCVDIKVFL K FNKIQQIL ...String:
MDEYLENTNL EELEQECFME DYQHEDVVEQ ENHQVDANDI YENQQMNDES QLNQDVKISQ QKEQAVEMIE EQQQNNQDKF KQFQDCMAH ITELNFKRNY QNLTEQSSSN NVVAEELDIK ESLKLQMEYY FCDTNLTHDS YLRGIISKSP KNCVDIKVFL K FNKIQQIL KQIQDKQIVS TYGIENQSQK KNHKNYKNQN ATFSKKDLIH LIRDSLKESK ILKVKMDSLK VKRRFPFNLE QA LKNSKQR TLYIDFLPPK CSKQTLVSIF GNFRIININL PLQKNSQLCQ GFAFIEFFSE EEANQALITK NSSIPKELIL LTE KKIGQG SIRIITYKKW QEEKQSFKEL SKNQNEQKNK NMNQSRKASD EFVSIDVEIK QNCLIKIINI PQGTLKAEVV LAVR HLGYE FYCDYIDENS NQINSNKISL STQQQNTAQC SNIQIENNLI QQDQHPQLND LLKEGQAMIR FQNSDEQRLA IQKLL NHNN NKLQIEIRGQ ICDVISTIPE DEEKNYWNYI KFKKNEFRKF FFMKKQQKKQ NITQNYNK

UniProtKB: La-related protein 7 homolog

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Macromolecule #5: RNA (159-MER)

MacromoleculeName: RNA (159-MER) / type: rna / ID: 5 / Number of copies: 1
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 50.746984 KDa
SequenceString:
AUACCCGCUU AAUUCAUUCA GAUCUGUAAU AGAACUGUCA UUCAACCCCA AAAAUCUAGU GCUGAUAUAA CCUUCACCAA UUAGGUUCA AAUAAGUGGU AAUGCGGGAC AAAAGACUAU CGACAUUUGA UACACUAUUU AUCAAUGGAU GUCUUAUUUU

GENBANK: GENBANK: AF399707.1

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Macromolecule #8: DNA (5'-D(P*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP...

MacromoleculeName: DNA (5'-D(P*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP*GP*TP*TP*GP*GP*GP*G)-3')
type: dna / ID: 8 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 6.059875 KDa
SequenceString:
(DG)(DT)(DT)(DG)(DG)(DG)(DG)(DT)(DT)(DG) (DG)(DG)(DG)(DT)(DT)(DG)(DG)(DG)(DG)

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Macromolecule #9: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 9 / Number of copies: 1 / 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

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 12.0 sec. / Average electron dose: 52.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: CTFFIND / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: EMDB MAP
EMDB ID:

6443

Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 52506
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION

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