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- EMDB-55321: Cryo-EM structure of yeast telomerase holoenzyme -

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Basic information

Entry
Database: EMDB / ID: EMD-55321
TitleCryo-EM structure of yeast telomerase holoenzyme
Map dataPost-processing map
Sample
  • Complex: Yeast telomerase holoenzyme
    • Complex: Yeast telomerase holoenzyme
      • Protein or peptide: Telomere replication protein EST3
      • Protein or peptide: Ribonucleases P/MRP protein subunit POP6
      • Protein or peptide: Telomere elongation protein EST1
      • Protein or peptide: Ribonucleases P/MRP protein subunit POP7
      • Protein or peptide: Ribonucleases P/MRP protein subunit POP1
      • RNA: TLC1 RNA
      • Protein or peptide: Telomerase reverse transcriptase
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION
  • Ligand: water
KeywordsTelomerase / Telomerase RNA / RNA BINDING PROTEIN
Function / homology
Function and homology information


nuclear-transcribed mRNA catabolic process, RNase MRP-dependent / intronic box C/D snoRNA processing / G-quadruplex DNA formation / nucleolar ribonuclease P complex / ribonuclease MRP complex / DNA/RNA helicase activity / telomerase catalytic core complex / ribonuclease P / telomerase activity / regulation of telomere maintenance via telomerase ...nuclear-transcribed mRNA catabolic process, RNase MRP-dependent / intronic box C/D snoRNA processing / G-quadruplex DNA formation / nucleolar ribonuclease P complex / ribonuclease MRP complex / DNA/RNA helicase activity / telomerase catalytic core complex / ribonuclease P / telomerase activity / regulation of telomere maintenance via telomerase / rRNA primary transcript binding / ribonuclease P activity / tRNA 5'-leader removal / telomerase holoenzyme complex / telomerase RNA binding / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / tRNA processing / maturation of 5.8S rRNA / telomeric repeat DNA binding / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / telomere maintenance via telomerase / telomere maintenance / RNA-directed DNA polymerase / rRNA processing / single-stranded DNA binding / chromosome, telomeric region / viral translational frameshifting / GTPase activity / nucleolus / RNA binding / metal ion binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Ribonuclease P/MRP subunit Pop7, fungi / Telomerase activating protein Est1-like, N-terminal / Telomerase activating protein Est1 / DNA/RNA-binding domain, Est1-type / Est1/Ebs1-like / Est1 DNA/RNA binding domain / Pop1, N-terminal / POPLD domain / Ribonucleases P/MRP protein subunit Pop1 / : ...Ribonuclease P/MRP subunit Pop7, fungi / Telomerase activating protein Est1-like, N-terminal / Telomerase activating protein Est1 / DNA/RNA-binding domain, Est1-type / Est1/Ebs1-like / Est1 DNA/RNA binding domain / Pop1, N-terminal / POPLD domain / Ribonucleases P/MRP protein subunit Pop1 / : / Ribonucleases P/MRP protein subunit POP1, N-terminal / POPLD (NUC188) domain / POP1 C-terminal domain / Ribonucleases P/MRP protein subunit Rpp20/Pop7 / Rpp20 subunit of nuclear RNase MRP and P / DNA/RNA-binding protein Alba-like / Alba / Alba-like domain superfamily / Shelterin complex subunit TPP1/Est3 / Shelterin complex subunit, TPP1/ACD / Telomerase ribonucleoprotein complex - RNA binding domain / Telomerase reverse transcriptase / Telomerase ribonucleoprotein complex - RNA-binding domain / Telomerase ribonucleoprotein complex - RNA binding domain / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Tetratricopeptide-like helical domain superfamily
Similarity search - Domain/homology
Telomere elongation protein EST1 / Ribonucleases P/MRP protein subunit POP7 / Ribonucleases P/MRP protein subunit POP1 / Ribonucleases P/MRP protein subunit POP6 / Telomere replication protein EST3 / Telomerase reverse transcriptase
Similarity search - Component
Biological speciesHomo sapiens (human) / Saccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsHu H / Franco-Echevarria E / Nguyen THD / Ahsan B / Oluwole A / Peak-Chew S / Robinson CV
Funding support United Kingdom, European Union, 2 items
OrganizationGrant numberCountry
UK Research and Innovation (UKRI)MC_UP_1201/19 United Kingdom
European Molecular Biology Organization (EMBO)European Union
CitationJournal: Science / Year: 2026
Title: Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.
Authors: Hongmiao Hu / Hannah Neumann / Gabriela M Teplitz / Elsa Franco-Echevarría / Pascal Chartrand / Raymund J Wellinger / Thi Hoang Duong Nguyen /
Abstract: Telomerase is a reverse transcriptase that synthesizes telomeric repeats at chromosome ends, safeguarding genome integrity. We present the cryo-electron microscopy structure of the budding yeast ...Telomerase is a reverse transcriptase that synthesizes telomeric repeats at chromosome ends, safeguarding genome integrity. We present the cryo-electron microscopy structure of the budding yeast telomerase, which exhibits substantial divergence from its ciliate and vertebrate counterparts. The structure reveals a stable core formed by telomerase RNA TLC1; the three ever shorter telomere (Est) proteins, Est1, Est2 and Est3; and the Pop1/Pop6/Pop7 complex (Pop1/6/7). TLC1, Est3, and Pop1/6/7 serve critical roles in complex assembly. We identified a zinc finger (ZnF) motif in the telomerase reverse transcriptase (TERT) subunit Est2 that is crucial for telomerase function. Structure prediction suggests the presence of ZnFs in TERT from diverse species. These findings offer insights into the functional organization of yeast telomerase and underscore the evolutionary diversity of telomerase holoenzymes.
History
DepositionOct 7, 2025-
Header (metadata) releaseApr 8, 2026-
Map releaseApr 8, 2026-
UpdateApr 8, 2026-
Current statusApr 8, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_55321.png

Downloads & links

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Map

FileDownload / File: emd_55321.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPost-processing map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.96 Å/pix.
x 360 pix.
= 343.8 Å		0.96 Å/pix.
x 360 pix.
= 343.8 Å		0.96 Å/pix.
x 360 pix.
= 343.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.955 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.9386962 - 2.123274
Average (Standard dev.)0.0052027986 (±0.045769572)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 343.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_55321_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Refinement half-map 1

Fileemd_55321_half_map_1.map
AnnotationRefinement half-map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Refinement half-map 2

Fileemd_55321_half_map_2.map
AnnotationRefinement half-map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Yeast telomerase holoenzyme

EntireName: Yeast telomerase holoenzyme
Components
  • Complex: Yeast telomerase holoenzyme
    • Complex: Yeast telomerase holoenzyme
      • Protein or peptide: Telomere replication protein EST3
      • Protein or peptide: Ribonucleases P/MRP protein subunit POP6
      • Protein or peptide: Telomere elongation protein EST1
      • Protein or peptide: Ribonucleases P/MRP protein subunit POP7
      • Protein or peptide: Ribonucleases P/MRP protein subunit POP1
      • RNA: TLC1 RNA
      • Protein or peptide: Telomerase reverse transcriptase
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION
  • Ligand: water

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Supramolecule #1: Yeast telomerase holoenzyme

SupramoleculeName: Yeast telomerase holoenzyme / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: Yeast telomerase holoenzyme

SupramoleculeName: Yeast telomerase holoenzyme / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#7
Details: Yeast telomerase holoenzyme consists of protein components: Est2, Est1, Est3, Pop1-6-7, Sm proteins,Ku70/80, and a RNA component TLC1
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: Telomere replication protein EST3

MacromoleculeName: Telomere replication protein EST3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 20.5775 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
MPKVILESHS KPTDSVFLQP WIKALIEDNS EHDQYHPSGH VIPSLTKQDL ALPHMSPTIL TNPCHFAKIT KFYNVCDYKV YASIRDSSH QILVEFSQEC VSNFERTHNC RITSETTNCL MIIGDADLVY VTNSRAMSHF KICLSNISSK EIVPVLNVNQ A TIFDIDQV GSLSTFPFVY KYL

UniProtKB: Telomere replication protein EST3

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Macromolecule #2: Ribonucleases P/MRP protein subunit POP6

MacromoleculeName: Ribonucleases P/MRP protein subunit POP6 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: ribonuclease P
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 18.234959 KDa
SequenceString:
MINGVYYNEI SRDLDISSST QCLRFLKETV IPSLANNGNN STSIQYHGIS KNDNIKKSVN KLDKQINMAD RSLGLQQVVC IFSYGPHIQ KMLSILEIFK KGYIKNNKKI YQWNKLTSFD IKREGRNELQ EERLKVPILV TLVSDSEIID LNLHSFTKQ

UniProtKB: Ribonucleases P/MRP protein subunit POP6

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Macromolecule #3: Telomere elongation protein EST1

MacromoleculeName: Telomere elongation protein EST1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 81.920938 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MDNEEVNEEC MRLFFKNARA HLDKHLTSRL TCDENAYITF RCFLDGIHRK STRFLEELLL KQENMYHNNN YERINDSVIP LVLKLLWLQ IHEPTLQWFE HWFHDIMRLS NRRKFRVFRI FQKKMIQFFK ITHRYYYDII EHLCAKYDMN SVISNALFAK L NLMQYTDG ...String:
MDNEEVNEEC MRLFFKNARA HLDKHLTSRL TCDENAYITF RCFLDGIHRK STRFLEELLL KQENMYHNNN YERINDSVIP LVLKLLWLQ IHEPTLQWFE HWFHDIMRLS NRRKFRVFRI FQKKMIQFFK ITHRYYYDII EHLCAKYDMN SVISNALFAK L NLMQYTDG LSTHEKIILN TSNPLTFSIV ISLQRCVINL GSTHFYKTLL NKPSNKPKSV EGFEKSIRYL NIASLYLPAV GD TYFQRAK IYLITGKFSL YFFELVRGAL VRIPSKCALN NLKDFILTPD FPERRRLMKK LAILVSKDLK GEKSFFEGQI VLQ FLSIVE HTLVPQSWNA SRASNCWLLK EHLQMAALKY HSGNINVILE NLAATMGSFD LMFTTRKSKE QKNKLKYADL SERQ VFFLD LSFDFIANII DVVIKPSWQK NMEDFRYLAI IRLLMCWIKS YRSILQYTHR HRKFCTSFAL LLNDLINSPL NCSGN IYSH RPKRSYLFRE DIIFREFSCI NFALTDFNDD YVYDSPDMIN NIIGCPTLTK VLSPKEECVL RIRSIIFSGM KFLEKN DTG VIWNASKYKF DLISPNIKIK RQIALSEISS KINVKTQQER VVSSRKVEAK RDEQQRKRAG KIAVTELEKQ FANVRRT KK LSPLPEKDGV SSELVKHAAS RGRKTITGPL SSDFLSYPDE AIDADEDITV QVPDTPT

UniProtKB: Telomere elongation protein EST1

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Macromolecule #4: Ribonucleases P/MRP protein subunit POP7

MacromoleculeName: Ribonucleases P/MRP protein subunit POP7 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: ribonuclease P
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 15.844284 KDa
SequenceString:
MALKKNTHNK STKRVTKHPS LKTLTHKQIH TTIFVKSTTP YVSALKRINK FLDSVHKQGS SYVAVLGMGK AVEKTLALGC HFQDQKNKK IEVYTKTIEV LDEVITEGQA DIDMESDVED DDKETQLKKR AVSGVELRIY V

UniProtKB: Ribonucleases P/MRP protein subunit POP7

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Macromolecule #5: Ribonucleases P/MRP protein subunit POP1

MacromoleculeName: Ribonucleases P/MRP protein subunit POP1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: ribonuclease P
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 100.559555 KDa
SequenceString: MSGSLSRGNG GKKVLNKNQL LKRNRIRNAR SIRAEAVAAS STKTGTPSDL SESGSKLNVD QFISSRQFEV KQLQLAMHNS KAASSTRIF QALPRKLRRR TASHNVRRIP KRMRNRALRE MRKSDQQDVL KGSSASSRKA HGLNAKQLYK ARMSIKLLRL A SKSTSMKL ...String:
MSGSLSRGNG GKKVLNKNQL LKRNRIRNAR SIRAEAVAAS STKTGTPSDL SESGSKLNVD QFISSRQFEV KQLQLAMHNS KAASSTRIF QALPRKLRRR TASHNVRRIP KRMRNRALRE MRKSDQQDVL KGSSASSRKA HGLNAKQLYK ARMSIKLLRL A SKSTSMKL SMPPEVTSSN CHVRQKIKTL KRMIKESSTA NPNIKLLNNR MGSYDCTGVN ELAPIPKGRV KYTKRQKHFA WL PTHIWNA KRSHMMKRWG YQMVWAPTQK CFKLTHRLGG DTCSSDGALC MDSSYIGTII VKDKSNDSEG DFLKSIIGKL TAE RANLRK YREGQVLFQG LIYSFNEENG EDSTKPLGPC DVFWVQKDTA IIRLHPSIYT QVFNILLQHK EKLTVQDCRY SLAS VTLKG AKALESLASC LRSTEYSKSF EQFKMVSMIT DHNALPQRCT FAFEAIDPRH LAAPKKLNDS QRKTVNSDDI LSLHE NYPQ DEINAVFNEL CDPESRTQSY NNQNTLKEIS ARRYKLLTAT PNSINKTTVP FKESDDPSIP LVIIRRLKTR DWIVVL PWF WLLPLWHLLN RIPRMYHIGL RQFQQIQYEN KQLYFPDDYP FTQLGYIENS FYKKEASKTK WDRKPMGKRI NFEKIKD IH NTKLPAYSGE IGDFFSSDWR FLQILRNGID YLQRNDKTLE LMDSKKTGQF NAQGVRDINC VNDVLEFCKD YEAKTKAM S LSIEENIPVA LCKNRKCQFR TPDSISVNSS SFSLTFFPRC IIAVSCTLLE RGHPKDNARI YQVPEKDLEH WLQLAKGVY RPNGRKDHDL KIPLPEVHDL IGFITSGTYH LNCGNGMGIG FIDHHAAIRQ PTRYVLIRNV GTNTYRLGEW SKISV

UniProtKB: Ribonucleases P/MRP protein subunit POP1

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Macromolecule #7: Telomerase reverse transcriptase

MacromoleculeName: Telomerase reverse transcriptase / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA-directed DNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 102.768094 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MKILFEFIQD KLDIDLQTNS TYKENLKCGH FNGLDEILTT CFALPNSRKI ALPCLPGDLS HKAVIDHCII YLLTGELYNN VLTFGYKIA RNEDVNNSLF CHSANVNVTL LKGAAWKMFH SLVGTYAFVD LLINYTVIQF NGQFFTQIVG NRCNEPHLPP K WAQRSSSS ...String:
MKILFEFIQD KLDIDLQTNS TYKENLKCGH FNGLDEILTT CFALPNSRKI ALPCLPGDLS HKAVIDHCII YLLTGELYNN VLTFGYKIA RNEDVNNSLF CHSANVNVTL LKGAAWKMFH SLVGTYAFVD LLINYTVIQF NGQFFTQIVG NRCNEPHLPP K WAQRSSSS SATAAQIKQL TEPVTNKQFL HKLNINSSSF FPYSKILPSS SSIKKLTDLR EAIFPTNLVK IPQRLKVRIN LT LQKLLKR HKRLNYVSIL NSICPPLEGT VLDLSHLSRQ SPKERVLKFI IVILQKLLPQ EMFGSKKNKG KIIKNLNLLL SLP LNGYLP FDSLLKKLRL KDFRWLFISD IWFTKHNFEN LNQLAICFIS WLFRQLIPKI IQTFFYCTEI SSTVTIVYFR HDTW NKLIT PFIVEYFKTY LVENNVCRNH NSYTLSNFNH SKMRIIPKKS NNEFRIIAIP CRGADEEEFT IYKENHKNAI QPTQK ILEY LRNKRPTSFT KIYSPTQIAD RIKEFKQRLL KKFNNVLPEL YFMKFDVKSC YDSIPRMECM RILKDALKNE NGFFVR SQY FFNTNTGVLK LFNVVNASRV PKPYELYIDN VRTVHLSNQD VINVVEMEIF KTALWVEDKC YIREDGLFQG SSLSAPI VD LVYDDLLEFY SEFKASPSQD TLILKLADDF LIISTDQQQV INIKKLAMGG FQKYNAKANR DKILAVSSQS DDDTVIQF C AMHIFVKELE VWKHSSTMNN FHIRSKSSKG IFRSLIALFN TRISYKTIDT NLNSTNTVLM QIDHVVKNIS ECYKSAFKD LSINVTQNMQ FHSFLQRIIE MTVSGCPITK CDPLIEYEVR FTILNGFLES LSSNTSKFKD NIILLRKEIQ HLQAYIYIYI HIVN

UniProtKB: Telomerase reverse transcriptase

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Macromolecule #6: TLC1 RNA

MacromoleculeName: TLC1 RNA / type: rna / ID: 6 / Number of copies: 1
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 370.246406 KDa
SequenceString: GAGAGGAAGA UAGGUACCCU AUGAAAAUGU CAAUGGCUGU UGCGUUUGCU UAAUCGUAUU UUUUUUUUUU UCAGUCCGUG UUUUUUGUA CAUUCUACGU UUGAGUUUUC CAUCAUGCAG GCCUCAGAAA UUUGGUAGGC ACUCGAUGGU GAAGAGAUAG U GUCGGAUU ...String:
GAGAGGAAGA UAGGUACCCU AUGAAAAUGU CAAUGGCUGU UGCGUUUGCU UAAUCGUAUU UUUUUUUUUU UCAGUCCGUG UUUUUUGUA CAUUCUACGU UUGAGUUUUC CAUCAUGCAG GCCUCAGAAA UUUGGUAGGC ACUCGAUGGU GAAGAGAUAG U GUCGGAUU UCGGAUUGAU CUUUCAGUUG AUAGCCUGCU GCUCUUUUCU UUUCCAAAGA AUUUCGAGUA UGCUGGUGUC AG UGUAGAU GCUUGUGUGU GCGCAAUUUG UGGUUUUUUA UUGUGUUUCU ACUUAUAGAU GGCUAAAAUC UGAGUUUAGA AAA UGCAAA CCGUAAAUUC UUAAACACUG CUAUUGCAUU UAGUUGCUAA AGCAGUGUUU UUGAACUUAU UCCUGUUAUU CCUU CUUCG UACCGAUCCU CUUCUCGACC UAACCUUUUA AUUACCAUGG GAAGCCUACC AUCACCACAC CCACACACAA AUGUU ACAG CUAAUUGUUU AUUAGCAAAG UUUGCACGAG UUCGCUGUUU AUUUUUUUCU CGUUUUCUUA UACCUAGUAU UUUUUC UGA CACUGUUUAA GGUGACAGAA AAAAAGGAGU UUAAGUUAGA UUUGCAAACA GACGGUGCUA AGCGCUGUCA CUUUAUG UC UAUCUUAUCG UUAACUCUGG AAAAAGAAAA AGGAAAAAGA ACGUCAGGGA ACAUGAGUAU AUAUAGAAAU GGUUUAUU C UAGUUUUUUC CGUUUUUUCA GUAGAUUUUU GCCUUUAAAA GAAUAAAUCC CACUACAAAA AGGUAAAAUA AAAAAUCUA UUCACUGAAC UUACUGAUGA AAUUUCCAAA UGUGCCCCGU ACAUCGAACG AUGUGACAGA GAAAAAUACG AGUAGGUAAA UAAGCCAAA AGGCAAGGGU GUCCUUUCUU AAGCAUCGGU UAGGUUUGCG GGCGAUCAGU AACUGAACAA UGACACAAGA U CAAGAACG UAAUUUGAGA UUUUUCAAGA UGGUUUUUUU AGGUAUCUAU UAAAACUACU UUGAUGAUCA AUACGGUAUU UU UGUCGCA UUAUUUUCCA AGCGGAAGGA ACCGUGUGUU CAUUUUAUGA AUCUUGGUGU UGUAUUCACA GCUACUUCUC CUA AUGCCU UCGAUGCAUU UAGAUAAUUU UUGGAAACAU U

GENBANK: GENBANK: U14595.1

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Macromolecule #8: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 8 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #9: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 9 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #10: water

MacromoleculeName: water / type: ligand / ID: 10 / Number of copies: 2 / 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: 8
Component:
ConcentrationFormulaName
150.0 mMNaClSodium chloride
20.0 mMC8H18N2O4SHEPES
2.0 mMMgCl2Magnesium chloride
1.0 %C3H8O3glycerol
0.05 %(C2H4O)nC14H22OIgepal CA-630
1.0 mMC4H10O2S2Dithiothreitol
0.2 mMC7H7FO2SPhenylmethanesulfonyl fluoride

Details: 150 mM NaCl, 20 mM HEPES NaOH pH 8.0, 2 mM MgCl2, 1% glycerol, 0.05% IGEPAL CA-630, 1 mM DTT, 0.2 mM PMSF
GridModel: UltrAuFoil R1.2/1.3 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV / Details: Blot Force: 10 Blot Time: 7.0 s Wait Time: 5 min.

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Electron microscopy

MicroscopeTFS KRIOS
TemperatureMin: 78.0 K
Specialist opticsEnergy filter - Name: TFS Selectris X / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 24936 / Average exposure time: 4.4 sec. / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / 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: 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

DetailsImages were processed using RELION5.0 and cryoSPARC
Particle selectionNumber selected: 1876851
CTF correctionSoftware - Name: cryoSPARC (ver. 4.5) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.5) / Number images used: 125104
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.5)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.5)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 4.5)
FSC plot (resolution estimation)

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