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- EMDB-40659: Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the ab... -

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Basic information

Entry
Database: EMDB / ID: EMD-40659
TitleCryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
Map dataSharpened full map of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
Sample
  • Complex: Human CST-POT1(ESDL)/TPP1 complex
    • Protein or peptide: CST complex subunit CTC1
    • Protein or peptide: CST complex subunit STN1
    • Protein or peptide: CST complex subunit TEN1
    • Protein or peptide: Protection of telomeres protein 1
  • Ligand: ZINC ION
Keywordstelomere / shelterin / cst / complex / DNA BINDING PROTEIN
Function / homology
Function and homology information


positive regulation of single-stranded telomeric DNA binding / positive regulation of DNA strand elongation / regulation of DNA helicase activity / positive regulation of DNA helicase activity / G-rich single-stranded DNA binding / telomere assembly / CST complex / segmentation / urogenital system development / positive regulation of helicase activity ...positive regulation of single-stranded telomeric DNA binding / positive regulation of DNA strand elongation / regulation of DNA helicase activity / positive regulation of DNA helicase activity / G-rich single-stranded DNA binding / telomere assembly / CST complex / segmentation / urogenital system development / positive regulation of helicase activity / 8-hydroxy-2'-deoxyguanosine DNA binding / regulation of double-strand break repair via nonhomologous end joining / telomeric D-loop binding / protection from non-homologous end joining at telomere / telomerase inhibitor activity / DEAD/H-box RNA helicase binding / establishment of protein localization to telomere / telomeric D-loop disassembly / telomere maintenance via telomere lengthening / shelterin complex / Telomere C-strand synthesis initiation / regulation of telomere maintenance via telomerase / telomere capping / Telomere C-strand (Lagging Strand) Synthesis / : / single-stranded telomeric DNA binding / positive regulation of telomere maintenance / nuclear telomere cap complex / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / Removal of the Flap Intermediate from the C-strand / G-rich strand telomeric DNA binding / telomerase holoenzyme complex / bone marrow development / embryonic limb morphogenesis / intermediate filament cytoskeleton / protein localization to chromosome, telomeric region / DNA duplex unwinding / hematopoietic stem cell proliferation / telomeric DNA binding / : / negative regulation of telomere maintenance via telomerase / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / telomere maintenance via telomerase / Telomere Extension By Telomerase / replicative senescence / carbohydrate transmembrane transporter activity / DNA polymerase binding / Packaging Of Telomere Ends / spleen development / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / regulation of G2/M transition of mitotic cell cycle / positive regulation of telomere maintenance via telomerase / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / telomere maintenance / Meiotic synapsis / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / bioluminescence / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / thymus development / positive regulation of DNA replication / T=pseudo3 icosahedral viral capsid / skeletal system development / generation of precursor metabolites and energy / intracellular protein transport / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / multicellular organism growth / DNA Damage/Telomere Stress Induced Senescence / endocytosis involved in viral entry into host cell / fibrillar center / positive regulation of fibroblast proliferation / nucleoside-triphosphate phosphatase / channel activity / single-stranded DNA binding / outer membrane-bounded periplasmic space / monoatomic ion transmembrane transport / chromosome, telomeric region / RNA helicase activity / nuclear body / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / intracellular membrane-bounded organelle / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / DNA damage response / protein-containing complex binding / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis
Similarity search - Function
CST complex subunit Ten1, animal and plant type / CST complex subunit CTC1 / CST complex subunit CTC1-like / CST, telomere maintenance, complex subunit CTC1 / Telomere-capping, CST complex subunit / CST complex subunit Stn1 / Stn1, C-terminal / CST complex subunit Stn1, wHTH1 motif superfamily / CST, complex subunit STN1, C terminal / : ...CST complex subunit Ten1, animal and plant type / CST complex subunit CTC1 / CST complex subunit CTC1-like / CST, telomere maintenance, complex subunit CTC1 / Telomere-capping, CST complex subunit / CST complex subunit Stn1 / Stn1, C-terminal / CST complex subunit Stn1, wHTH1 motif superfamily / CST, complex subunit STN1, C terminal / : / Protection of telomeres protein 1 (POT1), C-terminal insertion domain / Shelterin complex subunit TPP1/Est3 / Shelterin complex subunit, TPP1/ACD / Adrenocortical dysplasia protein / Protection of telomeres protein 1, ssDNA-binding domain / ssDNA-binding domain of telomere protection protein / Replication factor A protein-like / Protection of telomeres protein 1 / Telomeric single stranded DNA binding POT1/Cdc13 / Telomeric single stranded DNA binding POT1/CDC13 / Telomeric single stranded DNA binding POT1/CDC13 / OB-fold nucleic acid binding domain, AA-tRNA synthetase-type / OB-fold nucleic acid binding domain / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Picornavirus coat protein / Bacterial extracellular solute-binding protein / Green fluorescent protein, GFP / Bacterial extracellular solute-binding protein / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / Winged helix DNA-binding domain superfamily / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Winged helix-like DNA-binding domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Genome polyprotein / Maltose/maltodextrin-binding periplasmic protein / CST complex subunit CTC1 / CST complex subunit TEN1 / Adrenocortical dysplasia protein homolog / CST complex subunit STN1 / Protection of telomeres protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsCai SW
Funding support United States, 2 items
OrganizationGrant numberCountry
Other privateBCRF-22-036
National Institutes of Health/National Cancer Institute (NIH/NCI)R35 CA210036 United States
CitationJournal: bioRxiv / Year: 2023
Title: POT1 recruits and regulates CST-Polα/Primase at human telomeres.
Authors: Sarah W Cai / Hiroyuki Takai / Thomas Walz / Titia de Lange /
Abstract: Telomere maintenance requires extension of the G-rich telomeric repeat strand by telomerase and fill-in synthesis of the C-rich strand by Polα/Primase. Telomeric Polα/Primase is bound to Ctc1-Stn1- ...Telomere maintenance requires extension of the G-rich telomeric repeat strand by telomerase and fill-in synthesis of the C-rich strand by Polα/Primase. Telomeric Polα/Primase is bound to Ctc1-Stn1-Ten1 (CST), a single-stranded DNA-binding complex. Like mutations in telomerase, mutations affecting CST-Polα/Primase result in pathological telomere shortening and cause a telomere biology disorder, Coats plus (CP). We determined cryogenic electron microscopy structures of human CST bound to the shelterin heterodimer POT1/TPP1 that reveal how CST is recruited to telomeres by POT1. Phosphorylation of POT1 is required for CST recruitment, and the complex is formed through conserved interactions involving several residues mutated in CP. Our structural and biochemical data suggest that phosphorylated POT1 holds CST-Polα/Primase in an inactive auto-inhibited state until telomerase has extended the telomere ends. We propose that dephosphorylation of POT1 releases CST-Polα/Primase into an active state that completes telomere replication through fill-in synthesis.
History
DepositionApr 28, 2023-
Header (metadata) releaseJun 7, 2023-
Map releaseJun 7, 2023-
UpdateOct 16, 2024-
Current statusOct 16, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40659.png

Downloads & links

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Map

FileDownload / File: emd_40659.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened full map of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 352 pix.
= 302.72 Å		0.86 Å/pix.
x 352 pix.
= 302.72 Å		0.86 Å/pix.
x 352 pix.
= 302.72 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.86 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-1.4383488 - 2.3138247
Average (Standard dev.)0.0026847543 (±0.041630313)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions352352352
Spacing352352352
CellA=B=C: 302.72 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_40659_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A of human CST bound to...

Fileemd_40659_half_map_1.map
AnnotationHalf map A of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B of human CST bound to...

Fileemd_40659_half_map_2.map
AnnotationHalf map B of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human CST-POT1(ESDL)/TPP1 complex

EntireName: Human CST-POT1(ESDL)/TPP1 complex
Components
  • Complex: Human CST-POT1(ESDL)/TPP1 complex
    • Protein or peptide: CST complex subunit CTC1
    • Protein or peptide: CST complex subunit STN1
    • Protein or peptide: CST complex subunit TEN1
    • Protein or peptide: Protection of telomeres protein 1
  • Ligand: ZINC ION

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Supramolecule #1: Human CST-POT1(ESDL)/TPP1 complex

SupramoleculeName: Human CST-POT1(ESDL)/TPP1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 / Details: CST-POT1(ESDL)/TPP1 complex in the absence of DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 380 KDa

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Macromolecule #1: CST complex subunit CTC1

MacromoleculeName: CST complex subunit CTC1 / type: protein_or_peptide / ID: 1 / Details: His6-MBP-3C tagged human Ctc1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 178.300609 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MGSSHHHHHH SSGTKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGL LAEITPDKAF QDKLYPFTWD AVRYNGKLIA YPIAVEALSL IYNKDLLPNP PKTWEEIPAL DKELKAKGKS A LMFNLQEP ...String:
MGSSHHHHHH SSGTKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGL LAEITPDKAF QDKLYPFTWD AVRYNGKLIA YPIAVEALSL IYNKDLLPNP PKTWEEIPAL DKELKAKGKS A LMFNLQEP YFTWPLIAAD GGYAFKYENG KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE AAFNKGETAM TI NGPWAWS NIDTSKVNYG VTVLPTFKGQ PSKPFVGVLS AGINAASPNK ELAKEFLENY LLTDEGLEAV NKDKPLGAVA LKS YEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTKLVEKY LEVLFQGPGS MAAG RAQVP SSEQAWLEDA QVFIQKTLCP AVKEPNVQLT PLVIDCVKTV WLSQGRNQGS TLPLSYSFVS VQDLKTHQRL PCCSH LSWS SSAYQAWAQE AGPNGNPLPR EQLLLLGTLT DLSADLEQEC RNGSLYVRDN TGVLSCELID LDLSWLGHLF LFPRWS YLP PARWNSSGEG HLELWDAPVP VFPLTISPGP VTPIPVLYPE SASCLLRLRN KLRGVQRNLA GSLVRLSALV KSKQKAY FI LSLGRSHPAV THVSIIVQVP AQLVWHRALR PGTAYVLTEL RVSKIRGQRQ HVWMTSQSSR LLLLKPECVQ ELELELEG P LLEADPKPLP MPSNSEDKKD PESLVRYSRL LSYSGAVTGV LNEPAGLYEL DGQLGLCLAY QQFRGLRRVM RPGVCLQLQ DVHLLQSVGG GTRRPVLAPC LRGAVLLQSF SRQKPGAHSS RQAYGASLYE QLVWERQLGL PLYLWATKAL EELACKLCPH VLRHHQFLQ HSSPGSPSLG LQLLAPTLDL LAPPGSPVRN AHNEILEEPH HCPLQKYTRL QTPSSFPTLA TLKEEGQRKA W ASFDPKAL LPLPEASYLP SCQLNRRLAW SWLCLLPSAF CPAQVLLGVL VASSHKGCLQ LRDQSGSLPC LLLAKHSQPL SD PRLIGCL VRAERFQLIV ERDVRSSFPS WKELSMPGFI QKQQARVYVQ FFLADALILP VPRPCLHSAT PSTPQTDPTG PEG PHLGQS RLFLLCHKEA LMKRNFCVPP GASPEVPKPA LSFYVLGSWL GGTQRKEGTG WGLPEPQGND DNDQKVHLIF FGSS VRWFE FLHPGQVYRL IAPGPATPML FEKDGSSCIS RRPLELAGCA SCLTVQDNWT LELESSQDIQ DVLDANKSLP ESSLT DLLS DNFTDSLVSF SAEILSRTLC EPLVASLWMK LGNTGAMRRC VKLTVALETA ECEFPPHLDV YIEDPHLPPS LGLLPG ARV HFSQLEKRVS RSHNVYCCFR SSTYVQVLSF PPETTISIPL PHIYLAELLQ GGQSPFQATA SCHIVSVFSL QLFWVCA YC TSICRQGKCT RLGSTCPTQT AISQAIIRLL VEDGTAEAVV TCRNHHVAAA LGLCPREWAS LLDFVQVPGR VVLQFAGP G AQLESSARVD EPMTMFLWTL CTSPSVLRPI VLSFELERKP SKIVPLEPPR LQRFQCGELP FLTHVNPRLR LSCLSIRES EYSSSLGILA SSC

UniProtKB: Maltose/maltodextrin-binding periplasmic protein, CST complex subunit CTC1

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Macromolecule #2: CST complex subunit STN1

MacromoleculeName: CST complex subunit STN1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: picornain 2A
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 115.627211 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG SVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWP TLVTTLTYGV QCFSRYPDHM KQHDFFKSAM PEGYVQERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI D FKEDGNIL ...String:
MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG SVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWP TLVTTLTYGV QCFSRYPDHM KQHDFFKSAM PEGYVQERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI D FKEDGNIL GHKLEYNYNS HNVYIMADKQ KNGIKVNFKI RHNIEDGSVQ LADHYQQNTP IGDGPVLLPD NHYLSTQSAL SK DPNEKRD HMVLLEFVTA AGITLGMDEL YKENLYFQGG SMAGSGRLVL RPWIRELILG SETPSSPRAG QLLEVLQDAE AAV AGPSHA PDTSDVGATL LVSDGTHSVR CLVTREALDT SDWEEKEFGF RGTEGRLLLL QDCGVHVQVA EGGAPAEFYL QVDR FSLLP TEQPRLRVPG CNQDLDVQKK LYDCLEEHLS ESTSSNAGLS LSQLLDEMRE DQEHQGALVC LAESCLTLEG PCTAP PVTH WAASRCKATG EAVYTVPSSM LCISENDQLI LSSLGPCQRT QGPELPPPDP ALQDLSLTLI ASPPSSPSSS GTPALP GHM SSEESGTSIS LLPALSLAAP DPGQRSSSQP SPAICSAPAT LTPRSPHASR TPSSPLQSCT PSLSPRSHVP SPHQALV TR PQKPSLEFKE FVGLPCKNRP PFPRTGATRG AQEGGSGGSM QPGSSRCEEE TPSLLWGLDP VFLAFAKLYI RDILDMKE S RQVPGVFLYN GHPIKQVDVL GTVIGVRERD AFYSYGVDDS TGVINCICWK KLNTESVSAA PSAARELSLT SQLKKLQET IEQKTKIEIG DTIRVRGSIR TYREEREIHA TTYYKVDDPV WNIQIARMLE LPTIYRKVYD QPFHSSALEK EEALSNPGAL DLPSLTSLL SEKAKEFLME NRVQSFYQQE LEMVESLLSL ANQPVIHSAS SDQVNFKKDT TSKAIHSIFK NAIQLLQEKG L VFQKDDGF DNLYYVTRED KDLHRKIHRI IQQDCQKPNH MEKGCHFLHI LACARLSIRP GLSEAVLQQV LELLEDQSDI VS TMEHYYT AF

UniProtKB: Genome polyprotein, Adrenocortical dysplasia protein homolog, CST complex subunit STN1

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Macromolecule #3: CST complex subunit TEN1

MacromoleculeName: CST complex subunit TEN1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.872013 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MMLPKPGTYY LPWEVSAGQV PDGSTLRTFG RLCLYDMIQS RVTLMAQHGS DQHQVLVCTK LVEPFHAQVG SLYIVLGELQ HQQDRGSVV KARVLTCVEG MNLPLLEQAI REQRLYKQER GGSQ

UniProtKB: CST complex subunit TEN1

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Macromolecule #4: Protection of telomeres protein 1

MacromoleculeName: Protection of telomeres protein 1 / type: protein_or_peptide / ID: 4
Details: mPOT1b residues ESDL 323-326 are inserted into the human POT1 sequence between S320 and V321
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 72.938219 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHHHHHHGSS LVPATNYIYT PLNQLKGGTI VNVYGVVKFF KPPYLSKGTD YCSVVTIVDQ TNVKLTCLLF SGNYEALPII YKNGDIVRF HRLKIQVYKK ETQGITSSGF ASLTFEGTLG APIIPRTSSK YFNFTTEDHK MVEALRVWAS THMSPSWTLL K LCDVQPMQ ...String:
MHHHHHHGSS LVPATNYIYT PLNQLKGGTI VNVYGVVKFF KPPYLSKGTD YCSVVTIVDQ TNVKLTCLLF SGNYEALPII YKNGDIVRF HRLKIQVYKK ETQGITSSGF ASLTFEGTLG APIIPRTSSK YFNFTTEDHK MVEALRVWAS THMSPSWTLL K LCDVQPMQ YFDLTCQLLG KAEVDGASFL LKVWDGTRTP FPSWRVLIQD LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RS LKVGSFL RIYSLHTKLQ SMNSENQTML SLEFHLHGGT SYGRGIRVLP ESNSDVDQLK KDLESANLTA NQHSDVICQS EPD DSFPSS GSESDLVSLY EVERCQQLSA TILTDHQYLE RTPLCAILKQ KAPQQYRIRA KLRSYKPRRL FQSVKLHCPK CHLL QEVPH EGDLDIIFQD GATKTPDVKL QNTSLYDSKI WTTKNQKGRK VAVHFVKNNG ILPLSNECLL LIEGGTLSEI CKLSN KFNS VIPVRSGHED LELLDLSAPF LIQGTIHHYG CKQCSSLRSI QNLNSLVDKT SWIPSSVAEA LGIVPLQYVF VMTFTL DDG TGVLEAYLMD SDKFFQIPAS EVLMDDDLQK SVDMIMDMFC PPGIKIDAYP WLECFIKSYN VTNGTDNQIC YQIFDTT VA EDVI

UniProtKB: Protection of telomeres protein 1

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Macromolecule #5: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 5 / Number of copies: 2 / 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

Concentration0.05 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.3 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 132356
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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