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- EMDB-52976: Consensus dimer structure of human telomerase -

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Basic information

Entry
Database: EMDB / ID: EMD-52976
TitleConsensus dimer structure of human telomerase
Map dataSharpened cryoEM map for the consensus telomerase dimer.
Sample
  • Complex: Consensus dimer of human telomerase
    • Protein or peptide: x 9 types
    • RNA: x 1 types
    • DNA: x 1 types
KeywordsTelomerase / dimer / H/ACA RNP / catalytic core / reverse transcriptase / DNA BINDING PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.2 Å
AuthorsBalch S / Sekne Z / Franco-Echevarria E / Ludzia P / Kretsch RC / Sun W / Yu H / Ghanim GE / Sigurdur TR / Ding Y ...Balch S / Sekne Z / Franco-Echevarria E / Ludzia P / Kretsch RC / Sun W / Yu H / Ghanim GE / Sigurdur TR / Ding Y / Das R / Nguyen THD
Funding support United Kingdom, United States, European Union, China, 8 items
OrganizationGrant numberCountry
UK Research and Innovation (UKRI)MC_UP_1201/19 United Kingdom
Jane Coffin Childs (JCC) Fund United States
European Molecular Biology Organization (EMBO)European Union
Wellcome Trust226015/Z/22/Z United Kingdom
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)2R35GM122579 United States
Howard Hughes Medical Institute (HHMI) United States
Biotechnology and Biological Sciences Research Council (BBSRC)BB/X01102X/1 United Kingdom
Chinese Scholarship Council202206620047 China
CitationJournal: Science / Year: 2025
Title: Cryo-EM structure of human telomerase dimer reveals H/ACA RNP-mediated dimerization.
Authors: Sebastian Balch / Zala Sekne / Elsa Franco-Echevarría / Patryk Ludzia / Rachael C Kretsch / Wenqing Sun / Haopeng Yu / George E Ghanim / Sigurdur Thorkelsson / Yiliang Ding / Rhiju Das / ...Authors: Sebastian Balch / Zala Sekne / Elsa Franco-Echevarría / Patryk Ludzia / Rachael C Kretsch / Wenqing Sun / Haopeng Yu / George E Ghanim / Sigurdur Thorkelsson / Yiliang Ding / Rhiju Das / Thi Hoang Duong Nguyen /
Abstract: Telomerase ribonucleoprotein (RNP) synthesizes telomeric repeats at chromosome ends using a telomerase reverse transcriptase (TERT) and a telomerase RNA (hTR in humans). Previous structural work ...Telomerase ribonucleoprotein (RNP) synthesizes telomeric repeats at chromosome ends using a telomerase reverse transcriptase (TERT) and a telomerase RNA (hTR in humans). Previous structural work showed that human telomerase is typically monomeric, containing a single copy of TERT and hTR. Evidence for dimeric complexes exists, although the composition, high-resolution structure, and function remain elusive. Here, we report the cryo-electron microscopy (cryo-EM) structure of a human telomerase dimer bound to telomeric DNA. The structure reveals a 26-subunit assembly and a dimerization interface mediated by the Hinge and ACA box (H/ACA) RNP of telomerase. Premature aging disease mutations map to this interface. Disrupting dimer formation affects RNP assembly, bulk telomerase activity, and telomere maintenance in cells. Our findings address a long-standing enigma surrounding the telomerase dimer and suggest a role for the dimer in telomerase assembly.
History
DepositionFeb 28, 2025-
Header (metadata) releaseJul 16, 2025-
Map releaseJul 16, 2025-
UpdateJul 23, 2025-
Current statusJul 23, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52976.png

Downloads & links

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Map

FileDownload / File: emd_52976.map.gz / Format: CCP4 / Size: 59.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened cryoEM map for the consensus telomerase dimer.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.12 Å/pix.
x 250 pix.
= 529.5 Å		2.12 Å/pix.
x 250 pix.
= 529.5 Å		2.12 Å/pix.
x 250 pix.
= 529.5 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.118 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.3
Minimum - Maximum-1.5868534 - 5.4927526
Average (Standard dev.)0.017838893 (±0.21265952)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions250250250
Spacing250250250
CellA=B=C: 529.5 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: CryoEM map for the consensus telomerase dimer.

Fileemd_52976_additional_1.map
AnnotationCryoEM map for the consensus telomerase dimer.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2 for the consensus telomerase dimer.

Fileemd_52976_half_map_1.map
AnnotationHalf map 2 for the consensus telomerase dimer.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 1 for the consensus telomerase dimer.

Fileemd_52976_half_map_2.map
AnnotationHalf map 1 for the consensus telomerase dimer.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Consensus dimer of human telomerase

EntireName: Consensus dimer of human telomerase
Components
  • Complex: Consensus dimer of human telomerase
    • Protein or peptide: TERT, telomerase reverse transcriptase
    • RNA: hTR, human telomerase RNA
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • Protein or peptide: H/ACA ribonucleoprotein complex subunit DKC1, Dyskerin
    • Protein or peptide: H/ACA ribonucleoprotein complex subunit 1, GAR1
    • Protein or peptide: H/ACA ribonucleoprotein complex subunit 2, NHP2
    • Protein or peptide: H/ACA ribonucleoprotein complex subunit 3, NOP10
    • Protein or peptide: Telomerase Cajal body protein 1, TCAB1
    • DNA: DNA (5'-D(P*GP*TP*TP*AP*GP*GP*G)-3')
    • Protein or peptide: Adrenocortical dysplasia homolog, TPP1

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Supramolecule #1: Consensus dimer of human telomerase

SupramoleculeName: Consensus dimer of human telomerase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#11
Details: A full human telomerase dimer, composed of two H/ACA RNP lobes and two catalytic cores
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: TERT, telomerase reverse transcriptase

MacromoleculeName: TERT, telomerase reverse transcriptase / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO / EC number: RNA-directed DNA polymerase
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDPAAFRAL VAQCLVCVPW DARPPPAAPS FRQVSCLKEL VARVLQRLCE RGAKNVLAFG FALLDGARGG PPEAFTTSVR SYLPNTVTDA LRGSGAWGLL LRRVGDDVLV HLLARCALFV LVAPSCAYQV ...String:
MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDPAAFRAL VAQCLVCVPW DARPPPAAPS FRQVSCLKEL VARVLQRLCE RGAKNVLAFG FALLDGARGG PPEAFTTSVR SYLPNTVTDA LRGSGAWGLL LRRVGDDVLV HLLARCALFV LVAPSCAYQV CGPPLYQLGA ATQARPPPHA SGPRRRLGCE RAWNHSVREA GVPLGLPAPG ARRRGGSASR SLPLPKRPRR GAAPEPERTP VGQGSWAHPG RTRGPSDRGF CVVSPARPAE EATSLEGALS GTRHSHPSVG RQHHAGPPST SRPPRPWDTP CPPVYAETKH FLYSSGDKEQ LRPSFLLSSL RPSLTGARRL VETIFLGSRP WMPGTPRRLP RLPQRYWQMR PLFLELLGNH AQCPYGVLLK THCPLRAAVT PAAGVCAREK PQGSVAAPEE EDTDPRRLVQ LLRQHSSPWQ VYGFVRACLR RLVPPGLWGS RHNERRFLRN TKKFISLGKH AKLSLQELTW KMSVRDCAWL RRSPGVGCVP AAEHRLREEI LAKFLHWLMS VYVVELLRSF FYVTETTFQK NRLFFYRKSV WSKLQSIGIR QHLKRVQLRE LSEAEVRQHR EARPALLTSR LRFIPKPDGL RPIVNMDYVV GARTFRREKR AERLTSRVKA LFSVLNYERA RRPGLLGASV LGLDDIHRAW RTFVLRVRAQ DPPPELYFVK VDVTGAYDTI PQDRLTEVIA SIIKPQNTYC VRRYAVVQKA AHGHVRKAFK SHVSTLTDLQ PYMRQFVAHL QETSPLRDAV VIEQSSSLNE ASSGLFDVFL RFMCHHAVRI RGKSYVQCQG IPQGSILSTL LCSLCYGDME NKLFAGIRRD GLLLRLVDDF LLVTPHLTHA KTFLRTLVRG VPEYGCVVNL RKTVVNFPVE DEALGGTAFV QMPAHGLFPW CGLLLDTRTL EVQSDYSSYA RTSIRASLTF NRGFKAGRNM RRKLFGVLRL KCHSLFLDLQ VNSLQTVCTN IYKILLLQAY RFHACVLQLP FHQQVWKNPT FFLRVISDTA SLCYSILKAK NAGMSLGAKG AAGPLPSEAV QWLCHQAFLL KLTRHRVTYV PLLGSLRTAQ TQLSRKLPGT TLTALEAAAN PALPSDFKTI LD

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Macromolecule #3: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
SequenceString:
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VRRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK TESHHKAKGK

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Macromolecule #4: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
SequenceString:
MPDPAKSAPA PKKGSKKAVT KVQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSNPRNL SPTKPGGSED RQPPPSQLSA IPPFCLVLRA GIAGQV

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Macromolecule #5: H/ACA ribonucleoprotein complex subunit DKC1, Dyskerin

MacromoleculeName: H/ACA ribonucleoprotein complex subunit DKC1, Dyskerin
type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
SequenceString: ADAEVIILPK KHKKKKERKS LPEEDVAEIQ HAEEFLIKPE SKVAKLDTSQ WPLLLKNFDK LNVRTTHYTP LACGSNPLKR EIGDYIRTGF INLDKPSNPS SHEVVAWIRR ILRVEKTGHS GTLDPKVTGC LIVCIERATR LVKSQQSAGK EYVGIVRLHN AIEGGTQLSR ...String:
ADAEVIILPK KHKKKKERKS LPEEDVAEIQ HAEEFLIKPE SKVAKLDTSQ WPLLLKNFDK LNVRTTHYTP LACGSNPLKR EIGDYIRTGF INLDKPSNPS SHEVVAWIRR ILRVEKTGHS GTLDPKVTGC LIVCIERATR LVKSQQSAGK EYVGIVRLHN AIEGGTQLSR ALETLTGALF QRPPLIAAVK RQLRVRTIYE SKMIEYDPER RLGIFWVSCE AGTYIRTLCV HLGLLLGVGG QMQELRRVRS GVMSEKDHMV TMHDVLDAQW LYDNHKDESY LRRVVYPLEK LLTSHKRLVM KDSAVNAICY GAKIMLPGVL RYEDGIEVNQ EIVVITTKGE AICMAIALMT TAVISTCDHG IVAKIKRVIM ERDTYPRKWG LGPKASQKKL MIKQGLLDKH GKPTDSTPAT WKQEYVDYSE SAKKEVVAEV VKAPQVVAEA AKTAKRKRES ESESDETPPA APQLIKKEKK KSKKDKKAKA GLESGAEPGD GDSDTTKKKK KKKKAKEVEL VSE

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Macromolecule #6: H/ACA ribonucleoprotein complex subunit 1, GAR1

MacromoleculeName: H/ACA ribonucleoprotein complex subunit 1, GAR1 / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
SequenceString: MSFRGGGRGG FNRGGGGGGF NRGGSSNHFR GGGGGGGGGN FRGGGRGGFG RGGGRGGFNK GQDQGPPERV VLLGEFLHPC EDDIVCKCTT DENKVPYFNA PVYLENKEQI GKVDEIFGQL RDFYFSVKLS ENMKASSFKK LQKFYIDPYK LLPLQRFLPR PPGEKGPPRG ...String:
MSFRGGGRGG FNRGGGGGGF NRGGSSNHFR GGGGGGGGGN FRGGGRGGFG RGGGRGGFNK GQDQGPPERV VLLGEFLHPC EDDIVCKCTT DENKVPYFNA PVYLENKEQI GKVDEIFGQL RDFYFSVKLS ENMKASSFKK LQKFYIDPYK LLPLQRFLPR PPGEKGPPRG GGRGGRGGGR GGGGRGGGRG GGFRGGRGGG GGGFRGGRGG GFRGRGH

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Macromolecule #7: H/ACA ribonucleoprotein complex subunit 2, NHP2

MacromoleculeName: H/ACA ribonucleoprotein complex subunit 2, NHP2 / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
SequenceString:
MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED RNLPYVYIPS KTDLGAAAGS KRPTCVIMVK PHEEYQEAYD ECLEEVQSLP LPL

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Macromolecule #8: H/ACA ribonucleoprotein complex subunit 3, NOP10

MacromoleculeName: H/ACA ribonucleoprotein complex subunit 3, NOP10 / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
SequenceString:
MFLQYYLNEQ GDRVYTLKKF DPMGQQTCSA HPARFSPDDK YSRHRITIKK RFKVLMTQQP RPVL

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Macromolecule #9: Telomerase Cajal body protein 1, TCAB1

MacromoleculeName: Telomerase Cajal body protein 1, TCAB1 / type: protein_or_peptide / ID: 9 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
SequenceString: MKTLETQPLA PDCCPSDQDP APAHPSPHAS PMNKNADSEL MPPPPERGDP PRLSPDPVAG SAVSQELREG DPVSLSTPLE TEFGSPSELS PRIEEQELSE NTSLPAEEAN GSLSEEEANG PELGSGKAME DTSGEPAAED EGDTAWNYSF SQLPRFLSGS WSEFSTQPEN ...String:
MKTLETQPLA PDCCPSDQDP APAHPSPHAS PMNKNADSEL MPPPPERGDP PRLSPDPVAG SAVSQELREG DPVSLSTPLE TEFGSPSELS PRIEEQELSE NTSLPAEEAN GSLSEEEANG PELGSGKAME DTSGEPAAED EGDTAWNYSF SQLPRFLSGS WSEFSTQPEN FLKGCKWAPD GSCILTNSAD NILRIYNLPP ELYHEGEQVE YAEMVPVLRM VEGDTIYDYC WYSLMSSAQP DTSYVASSSR ENPIHIWDAF TGELRASFRA YNHLDELTAA HSLCFSPDGS QLFCGFNRTV RVFSTARPGR DCEVRATFAK KQGQSGIISC IAFSPAQPLY ACGSYGRSLG LYAWDDGSPL ALLGGHQGGI THLCFHPDGN RFFSGARKDA ELLCWDLRQS GYPLWSLGRE VTTNQRIYFD LDPTGQFLVS GSTSGAVSVW DTDGPGNDGK PEPVLSFLPQ KDCTNGVSLH PSLPLLATAS GQRVFPEPTE SGDEGEELGL PLLSTRHVHL ECRLQLWWCG GAPDSSIPDD HQGEKGQGGT EGGVGELI

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Macromolecule #11: Adrenocortical dysplasia homolog, TPP1

MacromoleculeName: Adrenocortical dysplasia homolog, TPP1 / type: protein_or_peptide / ID: 11 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera (butterflies/moths)
SequenceString: MAGSGRLVLR PWIRELILGS ETPSSPRAGQ LLEVLQDAEA AVAGPSHAPD TSDVGATLLV SDGTHSVRCL VTREALDTSD WEEKEFGFRG TEGRLLLLQD CGVHVQVAEG GAPAEFYLQV DRFSLLPTEQ PRLRVPGCNQ DLDVQKKLYD CLEEHLSEST SSNAGLSLSQ ...String:
MAGSGRLVLR PWIRELILGS ETPSSPRAGQ LLEVLQDAEA AVAGPSHAPD TSDVGATLLV SDGTHSVRCL VTREALDTSD WEEKEFGFRG TEGRLLLLQD CGVHVQVAEG GAPAEFYLQV DRFSLLPTEQ PRLRVPGCNQ DLDVQKKLYD CLEEHLSEST SSNAGLSLSQ LLDEMREDQE HQGALVCLAE SCLTLEGPCT APPVTHWAAS RCKATGEAVY TVPSSMLCIS ENDQLILSSL GPCQRTQGPE LPPPDPALQD LSLTLIASPP SSPSSSGTPA LPGHMSSEES GTSISLLPAL SLAAPDPGQR SSSQPSPAIC SAPATLTPRS PHASRTPSSP LQSCTPSLSP RSHVPSPHQA LVTRPQKPSL EFKEFVGLPC KNRPPFPRTG ATRGAQEPCS VWEPPKRHRD GSAFQYEYEP PCTSLCARVQ AVRLPPQLMA WALHFLMDAQ PGSEPTPM

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Macromolecule #2: hTR, human telomerase RNA

MacromoleculeName: hTR, human telomerase RNA / type: rna / ID: 2
Source (natural)Organism: Homo sapiens (human)
SequenceString: GGGUUGCGGA GGGUGGGCCU GGGAGGGGUG GUGGCCAUUU UUUGUCUAAC CCUAACUGAG AAGGGCGUAG GCGCCGUGCU UUUGCUCCCC GCGCGCUGUU UUUCUCGCUG ACUUUCAGCG GGCGGAAAAG CCUCGGCCUG CCGCCUUCCA CCGUUCAUUC UAGAGCAAAC ...String:
GGGUUGCGGA GGGUGGGCCU GGGAGGGGUG GUGGCCAUUU UUUGUCUAAC CCUAACUGAG AAGGGCGUAG GCGCCGUGCU UUUGCUCCCC GCGCGCUGUU UUUCUCGCUG ACUUUCAGCG GGCGGAAAAG CCUCGGCCUG CCGCCUUCCA CCGUUCAUUC UAGAGCAAAC AAAAAAUGUC AGCUGCUGGC CCGUUCGCCC CUCCCGGGGA CCUGCGGCGG GUCGCCUGCC CAGCCCCCGA ACCCCGCCUG GAGGCCGCGG UCGGCCCGGG GCUUCUCCGG AGGCACCCAC UGCCACCGCG AAGAGUUGGG CUCUGUCAGC CGCGGGUCUC UCGGGGGCGA GGGCGAGGUU CAGGCCUUUC AGGCCGCAGG AAGAGGAACG GAGCGAGUCC CCGCGCGCGG CGCGAUUCCC UGAGCUGUGG GACGUGCACC CAGGACUCGG CUCACACAUG C

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Macromolecule #10: DNA (5'-D(P*GP*TP*TP*AP*GP*GP*G)-3')

MacromoleculeName: DNA (5'-D(P*GP*TP*TP*AP*GP*GP*G)-3') / type: dna / ID: 10 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
SequenceString:
GTTAGGG

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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
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
150.0 mMNaClSodium Chloride
2.0 mMMgCl2Magnesium Chloride
0.05 %(C2H4O)nC14H22OIgepal CA630
1.0 %C12H22O11Trehalose
1.0 mMC4H10O2S2DTT
GridModel: C-flat / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 5 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 12 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
TemperatureMin: 78.0 K
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 4 / Number real images: 66992 / Average exposure time: 2.5 sec. / Average electron dose: 48.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated magnification: 45872 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000
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

DetailsAll images were processed using RELION 4.0, RELION 5.0 and CryoSPARC 4.1.2
Particle selectionNumber selected: 1871285
CTF correctionSoftware - Name: CTFFIND (ver. 4) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 6.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.1.2) / Number images used: 505039
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.1.2)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 4.1.2)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

8oue

source_name: PDB, initial_model_type: experimental model

7qxa

source_name: PDB, initial_model_type: experimental model
RefinementSpace: RECIPROCAL / Protocol: RIGID BODY FIT

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