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- EMDB-60534: Structure of CTF18-PCNA with ATP -

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Basic information

Entry
Database: EMDB / ID: EMD-60534
TitleStructure of CTF18-PCNA with ATP
Map dataThis is the sharpened map.
Sample
  • Complex: CTF18-PCNA
    • Protein or peptide: Chromosome transmission fidelity protein 18 homolog
    • Protein or peptide: Replication factor C subunit 2
    • Protein or peptide: Replication factor C subunit 5
    • Protein or peptide: Replication factor C subunit 4
    • Protein or peptide: Replication factor C subunit 3
    • Protein or peptide: Proliferating cell nuclear antigen
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsCTF18-RFC / human clamp loader / PCNA / sliding clamp / complex / ATP / DNA BINDING PROTEIN
Function / homology
Function and homology information


Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication / purine-specific mismatch base pair DNA N-glycosylase activity / DNA clamp loader activity / nuclear lamina ...Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / positive regulation of deoxyribonuclease activity / dinucleotide insertion or deletion binding / PCNA-p21 complex / mitotic telomere maintenance via semi-conservative replication / purine-specific mismatch base pair DNA N-glycosylase activity / DNA clamp loader activity / nuclear lamina / positive regulation of DNA-directed DNA polymerase activity / Polymerase switching / MutLalpha complex binding / Processive synthesis on the lagging strand / Telomere C-strand (Lagging Strand) Synthesis / PCNA complex / Removal of the Flap Intermediate / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Processive synthesis on the C-strand of the telomere / Transcription of E2F targets under negative control by DREAM complex / Polymerase switching on the C-strand of the telomere / Removal of the Flap Intermediate from the C-strand / replisome / response to L-glutamate / HDR through Single Strand Annealing (SSA) / DNA strand elongation involved in DNA replication / response to dexamethasone / DNA synthesis involved in DNA repair / Impaired BRCA2 binding to RAD51 / histone acetyltransferase binding / DNA polymerase processivity factor activity / G1/S-Specific Transcription / leading strand elongation / nuclear replication fork / replication fork processing / Presynaptic phase of homologous DNA pairing and strand exchange / SUMOylation of DNA replication proteins / PCNA-Dependent Long Patch Base Excision Repair / ATP-dependent activity, acting on DNA / response to cadmium ion / translesion synthesis / estrous cycle / mismatch repair / Activation of ATR in response to replication stress / cyclin-dependent protein kinase holoenzyme complex / base-excision repair, gap-filling / DNA polymerase binding / liver regeneration / epithelial cell differentiation / positive regulation of DNA repair / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / positive regulation of DNA replication / Gap-filling DNA repair synthesis and ligation in GG-NER / replication fork / nuclear estrogen receptor binding / male germ cell nucleus / Termination of translesion DNA synthesis / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / receptor tyrosine kinase binding / G2/M DNA damage checkpoint / HDR through Homologous Recombination (HRR) / Dual Incision in GG-NER / DNA-templated DNA replication / cellular response to xenobiotic stimulus / cellular response to hydrogen peroxide / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / cellular response to UV / response to estradiol / E3 ubiquitin ligases ubiquitinate target proteins / heart development / Processing of DNA double-strand break ends / chromatin organization / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / chromosome, telomeric region / DNA replication / nuclear body / DNA repair / centrosome / chromatin binding / chromatin / protein-containing complex binding / enzyme binding / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / cytosol
Similarity search - Function
: / Replication factor C subunit 3, C-terminal domain / RCF1/5-like, AAA+ ATPase lid domain / Replication factor C, C-terminal / Replication factor C C-terminal domain / : / DNA polymerase III, delta subunit / : / DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal / Proliferating cell nuclear antigen signature 2. ...: / Replication factor C subunit 3, C-terminal domain / RCF1/5-like, AAA+ ATPase lid domain / Replication factor C, C-terminal / Replication factor C C-terminal domain / : / DNA polymerase III, delta subunit / : / DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal / Proliferating cell nuclear antigen signature 2. / Proliferating cell nuclear antigen, PCNA, conserved site / Proliferating cell nuclear antigen signature 1. / Proliferating cell nuclear antigen, PCNA / Proliferating cell nuclear antigen, PCNA, N-terminal / Proliferating cell nuclear antigen, PCNA, C-terminal / Proliferating cell nuclear antigen, N-terminal domain / Proliferating cell nuclear antigen, C-terminal domain / : / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Proliferating cell nuclear antigen / Replication factor C subunit 4 / Replication factor C subunit 2 / Replication factor C subunit 5 / Replication factor C subunit 3 / Chromosome transmission fidelity protein 18 homolog
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.99 Å
AuthorsBriola GR / Tehseen M / Al-Amodi A / Nguyen PQ / Savva CG / Hamdan SM / De Biasio A
Funding support Saudi Arabia, 1 items
OrganizationGrant numberCountry
Other government Saudi Arabia
CitationJournal: bioRxiv / Year: 2025
Title: Structure of the human CTF18-RFC clamp loader bound to PCNA.
Authors: Giuseppina R Briola / Muhammad Tehseen / Amani Al-Amodi / Grace Young / Ammar U Danazumi / Phong Quoc Nguyen / Christos G Savva / Mark Hedglin / Samir M Hamdan / Alfredo De Biasio /
Abstract: Sliding clamps like PCNA are crucial processivity factors for replicative polymerases, requiring specific clamp loaders for loading onto DNA. The human alternative clamp loader CTF18-RFC interacts ...Sliding clamps like PCNA are crucial processivity factors for replicative polymerases, requiring specific clamp loaders for loading onto DNA. The human alternative clamp loader CTF18-RFC interacts with the leading strand polymerase Pol ε and loads PCNA onto primer/template DNA using its RFC pentameric module. Here, we provide a structural characterization of the human CTF18-RFC complex and its interaction with PCNA. Our cryo-EM data support that the Ctf8 and Dcc1 subunits of CTF18-RFC, which form the regulatory module interacting with Pol ε, are flexibly tethered to the RFC module. A 2.9 Å cryo-EM structure shows the RFC module bound to PCNA in an auto-inhibited conformation similar to the canonical RFC loader, marking the initial step of the clamp-loading reaction. The unique RFC1 (Ctf18) large subunit of CTF18-RFC, which based on the cryo-EM map shows high relative flexibility, is anchored to PCNA through an atypical low-affinity PIP box in the AAA+ domain and engages the RFC5 subunit using a novel β-hairpin at the disordered N-terminus. We show that deletion of this β-hairpin impairs the CTF18-RFC-PCNA complex stability, slows down clamp loading, and decreases the rate of primer synthesis by Pol ε. Our research identifies distinctive structural characteristics of the human CTF18-RFC complex, providing insights into its role in PCNA loading and the stimulation of leading strand synthesis by Pol ε.
History
DepositionJun 13, 2024-
Header (metadata) releaseJun 18, 2025-
Map releaseJun 18, 2025-
UpdateAug 27, 2025-
Current statusAug 27, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_60534.png

Downloads & links

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Map

FileDownload / File: emd_60534.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThis is the sharpened map.
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.93 Å/pix.
x 480 pix.
= 446.4 Å		0.93 Å/pix.
x 480 pix.
= 446.4 Å		0.93 Å/pix.
x 480 pix.
= 446.4 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.93 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.006
Minimum - Maximum-0.030227788 - 0.06433667
Average (Standard dev.)0.000021649657 (±0.00065258914)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 446.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_60534_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 1.

Fileemd_60534_half_map_1.map
AnnotationHalf map 1.
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2.

Fileemd_60534_half_map_2.map
AnnotationHalf map 2.
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : CTF18-PCNA

EntireName: CTF18-PCNA
Components
  • Complex: CTF18-PCNA
    • Protein or peptide: Chromosome transmission fidelity protein 18 homolog
    • Protein or peptide: Replication factor C subunit 2
    • Protein or peptide: Replication factor C subunit 5
    • Protein or peptide: Replication factor C subunit 4
    • Protein or peptide: Replication factor C subunit 3
    • Protein or peptide: Proliferating cell nuclear antigen
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: CTF18-PCNA

SupramoleculeName: CTF18-PCNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6 / Details: CTF18 in complex with PCNA, in presence of ATP
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 323 KDa

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Macromolecule #1: Chromosome transmission fidelity protein 18 homolog

MacromoleculeName: Chromosome transmission fidelity protein 18 homolog / type: protein_or_peptide / ID: 1
Details: 8ZWO: -35 INITIAL M 8ZWO: from -34 to 0 is the expression tag
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 111.40707 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KENLYFQGED YEQELCGVED DFHNQFAAEL EVLAELEGAS TPSPSGVPLF TAGRPPRTF EEALARGDAA SSPAPAASVG SSQGGARKRQ VDADLQPAGS LPHAPRIKRP RLQVVKRLNF RSEEMEEPPP P DSSPTDIT ...String:
MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KENLYFQGED YEQELCGVED DFHNQFAAEL EVLAELEGAS TPSPSGVPLF TAGRPPRTF EEALARGDAA SSPAPAASVG SSQGGARKRQ VDADLQPAGS LPHAPRIKRP RLQVVKRLNF RSEEMEEPPP P DSSPTDIT PPPSPEDLAE LWGHGVSEAA ADVGLTRASP AARNPVLRRP PILEDYVHVT STEGVRAYLV LRADPMAPGV QG SLLHVPW RGGGQLDLLG VSLASLKKQV DGERRERLLQ EAQKLSDTLH SLRSGEEEAA QPLGAPEEEP TDGQDASSHC LWV DEFAPR HYTELLSDDF TNRCLLKWLK LWDLVVFGHE RPSRKPRPSV EPARVSKEAT APGKWKSHEQ VLEEMLEAGL DPSQ RPKQK VALLCGPPGL GKTTLAHVIA RHAGYSVVEM NASDDRSPEV FRTRIEAATQ MESVLGAGGK PNCLVIDEID GAPVA AINV LLSILNRKGP QEVGPQGPAV PSGGGRRRRA EGGLLMRPII CICNDQFAPS LRQLKQQAFL LHFPPTLPSR LVQRLQ EVS LRQGMRADPG VLAALCEKTD NDIRACINTL QFLYSRGQRE LSVRDVQATR VGLKDQRRGL FSVWQEVFQL PRAQRRR VG QDPALPADTL LLGDGDAGSL TSASQRFYRV LHAAASAGEH EKVVQGLFDN FLRLRLRDSS LGAVCVALDW LAFDDLLA G AAHHSQSFQL LRYPPFLPVA FHVLFASSHT PRITFPSSQQ EAQNRMSQMR NLIQTLVSGI APATRSRATP QALLLDALC LLLDILAPKL RPVSTQLYST REKQQLASLV GTMLAYSLTY RQERTPDGQY IYRLEPNVEE LCRFPELPAR KPLTYQTKQL IAREIEVEK MRRAEASARV ENSPQVDGSP PGLEGLLGGI GEKGVHRPAP RNHEQRLEHI MRRAAREEQP EKDFFGRVVV R STAVPSAG DTAPEQDSVE RRMGTAVGRS EVWFRFNEGV SNAVRRSLYI RDLL

UniProtKB: Chromosome transmission fidelity protein 18 homolog

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Macromolecule #2: Replication factor C subunit 2

MacromoleculeName: Replication factor C subunit 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.203207 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI VGNEDTVSRL EVFAREGNVP NIIIAGPPGT GKTTSILCL ARALLGPALK DAMLELNASN DRGIDVVRNK IKMFAQQKVT LPKGRHKIII LDEADSMTDG AQQALRRTME I YSKTTRFA ...String:
MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI VGNEDTVSRL EVFAREGNVP NIIIAGPPGT GKTTSILCL ARALLGPALK DAMLELNASN DRGIDVVRNK IKMFAQQKVT LPKGRHKIII LDEADSMTDG AQQALRRTME I YSKTTRFA LACNASDKII EPIQSRCAVL RYTKLTDAQI LTRLMNVIEK ERVPYTDDGL EAIIFTAQGD MRQALNNLQS TF SGFGFIN SENVFKVCDE PHPLLVKEMI QHCVNANIDE AYKILAHLWH LGYSPEDIIG NIFRVCKTFQ MAEYLKLEFI KEI GYTHMK IAEGVNSLLQ MAGLLARLCQ KTMAPVAS

UniProtKB: Replication factor C subunit 2

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Macromolecule #3: Replication factor C subunit 5

MacromoleculeName: Replication factor C subunit 5 / type: protein_or_peptide / ID: 3
Details: 8ZWO: M-5 INITIATING METHIONINE 8ZWO: from -4 to 0 is the expression tag
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 38.545512 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: METSALKQQE QPAATKIRNL PWVEKYRPQT LNDLISHQDI LSTIQKFINE DRLPHLLLYG PPGTGKTSTI LACAKQLYKD KEFGSMVLE LNASDDRGID IIRGPILSFA STRTIFKKGF KLVILDEADA MTQDAQNALR RVIEKFTENT RFCLICNYLS K IIPALQSR ...String:
METSALKQQE QPAATKIRNL PWVEKYRPQT LNDLISHQDI LSTIQKFINE DRLPHLLLYG PPGTGKTSTI LACAKQLYKD KEFGSMVLE LNASDDRGID IIRGPILSFA STRTIFKKGF KLVILDEADA MTQDAQNALR RVIEKFTENT RFCLICNYLS K IIPALQSR CTRFRFGPLT PELMVPRLEH VVEEEKVDIS EDGMKALVTL SSGDMRRALN ILQSTNMAFG KVTEETVYTC TG HPLKSDI ANILDWMLNQ DFTTAYRNIT ELKTLKGLAL HDILTEIHLF VHRVDFPSSV RIHLLTKMAD IEYRLSVGTN EKI QLSSLI AAFQVTRDLI VAEA

UniProtKB: Replication factor C subunit 5

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Macromolecule #4: Replication factor C subunit 4

MacromoleculeName: Replication factor C subunit 4 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.735711 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MQAFLKGTSI STKPPLTKDR GVAASAGSSG ENKKAKPVPW VEKYRPKCVD EVAFQEEVVA VLKKSLEGAD LPNLLFYGPP GTGKTSTIL AAARELFGPE LFRLRVLELN ASDERGIQVV REKVKNFAQL TVSGSRSDGK PCPPFKIVIL DEADSMTSAA Q AALRRTME ...String:
MQAFLKGTSI STKPPLTKDR GVAASAGSSG ENKKAKPVPW VEKYRPKCVD EVAFQEEVVA VLKKSLEGAD LPNLLFYGPP GTGKTSTIL AAARELFGPE LFRLRVLELN ASDERGIQVV REKVKNFAQL TVSGSRSDGK PCPPFKIVIL DEADSMTSAA Q AALRRTME KESKTTRFCL ICNYVSRIIE PLTSRCSKFR FKPLSDKIQQ QRLLDIAKKE NVKISDEGIA YLVKVSEGDL RK AITFLQS ATRLTGGKEI TEKVITDIAG VIPAEKIDGV FAACQSGSFD KLEAVVKDLI DEGHAATQLV NQLHDVVVEN NLS DKQKSI ITEKLAEVDK CLADGADEHL QLISLCATVM QQLSQNC

UniProtKB: Replication factor C subunit 4

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Macromolecule #5: Replication factor C subunit 3

MacromoleculeName: Replication factor C subunit 3 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.436258 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MHHHHHMSLW VDKYRPCSLG RLDYHKEQAA QLRNLVQCGD FPHLLVYGPS GAGKKTRIMC ILRELYGVGV EKLRIEHQTI TTPSKKKIE ISTIASNYHL EVNPSDAGNS DRVVIQEMLK TVAQSQQLET NSQRDFKVVL LTEVDKLTKD AQHALRRTME K YMSTCRLI ...String:
MHHHHHMSLW VDKYRPCSLG RLDYHKEQAA QLRNLVQCGD FPHLLVYGPS GAGKKTRIMC ILRELYGVGV EKLRIEHQTI TTPSKKKIE ISTIASNYHL EVNPSDAGNS DRVVIQEMLK TVAQSQQLET NSQRDFKVVL LTEVDKLTKD AQHALRRTME K YMSTCRLI LCCNSTSKVI PPIRSRCLAV RVPAPSIEDI CHVLSTVCKK EGLNLPSQLA HRLAEKSCRN LRKALLMCEA CR VQQYPFT ADQEIPETDW EVYLRETANA IVSQQTPQRL LEVRGRLYEL LTHCIPPEII MKGLLSELLH NCDGQLKGEV AQM AAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG LEGMMF

UniProtKB: Replication factor C subunit 3

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Macromolecule #6: Proliferating cell nuclear antigen

MacromoleculeName: Proliferating cell nuclear antigen / type: protein_or_peptide / ID: 6
Details: 8ZWO: M -5, initiation metihionine 8ZWO: -4 to 0, expression tag
Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.617672 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHMFEA RLVQGSILKK VLEALKDLIN EACWDISSSG VNLQSMDSSH VSLVQLTLRS EGFDTYRCDR NLAMGVNLTS MSKILKCAG NEDIITLRAE DNADTLALVF EAPNQEKVSD YEMKLMDLDV EQLGIPEQEY SCVVKMPSGE FARICRDLSH I GDAVVISC ...String:
MHHHHHMFEA RLVQGSILKK VLEALKDLIN EACWDISSSG VNLQSMDSSH VSLVQLTLRS EGFDTYRCDR NLAMGVNLTS MSKILKCAG NEDIITLRAE DNADTLALVF EAPNQEKVSD YEMKLMDLDV EQLGIPEQEY SCVVKMPSGE FARICRDLSH I GDAVVISC AKDGVKFSAS GELGNGNIKL SQTSNVDKEE EAVTIEMNEP VQLTFALRYL NFFTKATPLS STVTLSMSAD VP LVVEYKI ADMGHLKYYL APKIEDEEGS

UniProtKB: Proliferating cell nuclear antigen

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Macromolecule #7: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 3 / 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 #8: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 8 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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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: 7.5 / Details: 50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Details: 30 mA
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
TemperatureMin: 83.0 K
Specialist opticsEnergy filter - Name: TFS Selectris X / Energy filter - Slit width: 10 eV
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 1 / Number real images: 7907 / Average exposure time: 5.0 sec. / Average electron dose: 43.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.7 µm / Nominal defocus min: 1.5 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: 2043120
CTF correctionSoftware - Name: RELION (ver. 4.0) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionNumber classes used: 2 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.99 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0) / Number images used: 527527
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6vvo


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-8zwo:
Structure of CTF18-PCNA with ATP

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