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- EMDB-52960: Cryo-EM structure of human Mre11-Rad50-Nbs1 complex bound to DNA -

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Basic information

Entry
Database: EMDB / ID: EMD-52960
TitleCryo-EM structure of human Mre11-Rad50-Nbs1 complex bound to DNA
Map data
Sample
  • Complex: Mre11-Rad50-Nbs1-DNA complex
    • DNA: DNA (50-MER)
    • DNA: DNA (50-MER)
    • Protein or peptide: Nibrin
    • Protein or peptide: DNA repair protein RAD50
    • Protein or peptide: Double-strand break repair protein MRE11
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: BERYLLIUM TRIFLUORIDE ION
  • Ligand: MANGANESE (II) ION
  • Ligand: water
KeywordsMre11-Rad50-Nbs1 complex / double-strand DNA break repair protein / nuclease / HYDROLASE
Function / homology
Function and homology information


telomere maintenance via telomere trimming / chromosomal region / telomeric 3' overhang formation / mitochondrial double-strand break repair via homologous recombination / Mre11 complex / negative regulation of double-strand break repair via nonhomologous end joining / blastocyst growth / negative regulation of telomere capping / BRCA1-C complex / Sensing of DNA Double Strand Breaks ...telomere maintenance via telomere trimming / chromosomal region / telomeric 3' overhang formation / mitochondrial double-strand break repair via homologous recombination / Mre11 complex / negative regulation of double-strand break repair via nonhomologous end joining / blastocyst growth / negative regulation of telomere capping / BRCA1-C complex / Sensing of DNA Double Strand Breaks / meiotic DNA double-strand break formation / protection from non-homologous end joining at telomere / regulation of mitotic recombination / R-loop processing / Hydrolases; Acting on acid anhydrides / t-circle formation / single-stranded DNA endodeoxyribonuclease activity / chromosome organization involved in meiotic cell cycle / phosphorylation-dependent protein binding / homologous chromosome pairing at meiosis / double-stranded telomeric DNA binding / DNA strand resection involved in replication fork processing / nuclease activity / homologous recombination / G-quadruplex DNA binding / nuclear inclusion body / 3'-5'-DNA exonuclease activity / DNA double-strand break processing / single-stranded telomeric DNA binding / Impaired BRCA2 binding to PALB2 / double-strand break repair via alternative nonhomologous end joining / chromatin-protein adaptor activity / protein localization to site of double-strand break / telomere maintenance via recombination / isotype switching / Cytosolic sensors of pathogen-associated DNA / mitotic G2/M transition checkpoint / HDR through MMEJ (alt-NHEJ) / IRF3-mediated induction of type I IFN / reciprocal meiotic recombination / mitotic intra-S DNA damage checkpoint signaling / regulation of DNA-templated DNA replication initiation / sister chromatid cohesion / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / HDR through Single Strand Annealing (SSA) / neuromuscular process controlling balance / positive regulation of double-strand break repair / Impaired BRCA2 binding to RAD51 / mitotic G2 DNA damage checkpoint signaling / positive regulation of telomere maintenance / telomere maintenance in response to DNA damage / Presynaptic phase of homologous DNA pairing and strand exchange / protein K63-linked ubiquitination / neuroblast proliferation / telomere maintenance via telomerase / positive regulation of double-strand break repair via homologous recombination / 3'-5' exonuclease activity / telomere maintenance / intrinsic apoptotic signaling pathway / DNA damage checkpoint signaling / replication fork / protein serine/threonine kinase activator activity / condensed nuclear chromosome / DNA endonuclease activity / meiotic cell cycle / double-strand break repair via homologous recombination / DNA damage response, signal transduction by p53 class mediator / Nonhomologous End-Joining (NHEJ) / HDR through Homologous Recombination (HRR) / G2/M DNA damage checkpoint / PML body / DNA Damage/Telomere Stress Induced Senescence / double-strand break repair via nonhomologous end joining / Meiotic recombination / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / site of double-strand break / double-strand break repair / manganese ion binding / Processing of DNA double-strand break ends / double-stranded DNA binding / Regulation of TP53 Activity through Phosphorylation / histone binding / protein-macromolecule adaptor activity / DNA recombination / damaged DNA binding / DNA-binding transcription factor binding / Hydrolases; Acting on ester bonds / chromosome, telomeric region / cell population proliferation / regulation of cell cycle / cadherin binding / DNA repair / DNA damage response / negative regulation of apoptotic process / nucleolus
Similarity search - Function
Nibrin, C-terminal / Nibrin / DNA damage repair protein Nbs1 / DNA damage repair protein Nbs1 / Nibrin, second BRCT domain / Nibrin, second BRCT domain superfamily / Second BRCT domain on Nijmegen syndrome breakage protein / DNA repair protein Rad50, eukaryotes / Nibrin-related / DNA double-strand break repair protein Mre11 ...Nibrin, C-terminal / Nibrin / DNA damage repair protein Nbs1 / DNA damage repair protein Nbs1 / Nibrin, second BRCT domain / Nibrin, second BRCT domain superfamily / Second BRCT domain on Nijmegen syndrome breakage protein / DNA repair protein Rad50, eukaryotes / Nibrin-related / DNA double-strand break repair protein Mre11 / Mre11, DNA-binding / Mre11, capping domain / Mre11 DNA-binding presumed domain / Mre11 DNA-binding presumed domain / Rad50 zinc hook motif / RAD50, zinc hook / Rad50 zinc-hook domain profile. / Mre11 nuclease, N-terminal metallophosphatase domain / SbcC/RAD50-like, Walker B motif / Rad50/SbcC-type AAA domain / AAA domain / Forkhead associated domain / Forkhead-associated (FHA) domain profile. / FHA domain / Forkhead-associated (FHA) domain / SMAD/FHA domain superfamily / BRCA1 C Terminus (BRCT) domain / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / BRCT domain / BRCT domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Nibrin / Double-strand break repair protein MRE11 / DNA repair protein RAD50
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.79 Å
AuthorsCui HJ / Lammens K / Hopfner KP / Fan YL / Kuybu F
Funding support Germany, 1 items
OrganizationGrant numberCountry
German Research Foundation (DFG) Germany
CitationJournal: Nat Commun / Year: 2025
Title: Structural basis for DNA break sensing by human MRE11-RAD50-NBS1 and its regulation by telomeric factor TRF2.
Authors: Yilan Fan / Filiz Kuybu / Hengjun Cui / Katja Lammens / Jia-Xuan Chen / Michael Kugler / Christophe Jung / Karl-Peter Hopfner /
Abstract: The MRE11-RAD50-NBS1 (MRN) complex is a central, multifunctional factor in the detection, signaling and nucleolytic processing of DNA double-strand breaks (DSBs). To clarify how human MRN binds ...The MRE11-RAD50-NBS1 (MRN) complex is a central, multifunctional factor in the detection, signaling and nucleolytic processing of DNA double-strand breaks (DSBs). To clarify how human MRN binds generic and telomeric DNA ends and can separate DNA end sensing from nuclease activities, we determined cryo-electron microscopy (cryo-EM) structures of human MRN bound to DNA and to DNA and the telomere protection factor TRF2. MRN senses DSBs through a tight clamp-like sensing state with closed coiled-coil domains, but auto-inhibited MRE11 nuclease. NBS1 wraps around the MRE11 dimer, with NBS1's ATM recruitment motif sequestered by binding to the regulatory RAD50 S site, necessitating a switch in the NBS1 C helix for ATM activation. At telomeric DNA, TRF2 blocks the second S site via the iDDR motif to prevent nuclease and ATM activation. Our results provide a structural framework for DNA sensing via a gating mechanism and separation of sensing, signaling and processing activities of mammalian MRN.
History
DepositionFeb 26, 2025-
Header (metadata) releaseOct 1, 2025-
Map releaseOct 1, 2025-
UpdateOct 1, 2025-
Current statusOct 1, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52960.png

Downloads & links

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Map

FileDownload / File: emd_52960.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
0.73 Å/pix.
x 360 pix.
= 261.72 Å		0.73 Å/pix.
x 360 pix.
= 261.72 Å		0.73 Å/pix.
x 360 pix.
= 261.72 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.727 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum-1.3577906 - 2.221706
Average (Standard dev.)0.0010383598 (±0.06523449)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 261.72 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_52960_msk_1.map
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Half map: #2

Fileemd_52960_half_map_1.map
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Half map: #1

Fileemd_52960_half_map_2.map
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Sample components

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Entire : Mre11-Rad50-Nbs1-DNA complex

EntireName: Mre11-Rad50-Nbs1-DNA complex
Components
  • Complex: Mre11-Rad50-Nbs1-DNA complex
    • DNA: DNA (50-MER)
    • DNA: DNA (50-MER)
    • Protein or peptide: Nibrin
    • Protein or peptide: DNA repair protein RAD50
    • Protein or peptide: Double-strand break repair protein MRE11
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: BERYLLIUM TRIFLUORIDE ION
  • Ligand: MANGANESE (II) ION
  • Ligand: water

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Supramolecule #1: Mre11-Rad50-Nbs1-DNA complex

SupramoleculeName: Mre11-Rad50-Nbs1-DNA complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 592 KDa

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Macromolecule #1: DNA (50-MER)

MacromoleculeName: DNA (50-MER) / type: dna / ID: 1 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.164683 KDa
SequenceString:
(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT) (DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)

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Macromolecule #2: DNA (50-MER)

MacromoleculeName: DNA (50-MER) / type: dna / ID: 2 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.615376 KDa
SequenceString:
(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)

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Macromolecule #3: Nibrin

MacromoleculeName: Nibrin / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 85.073023 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MWKLLPAAGP AGGEPYRLLT GVEYVVGRKN CAILIENDQS ISRNHAVLTA NFSVTNLSQT DEIPVLTLKD NSKYGTFVNE EKMQNGFSR TLKSGDGITF GVFGSKFRIE YEPLVACSSC LDVSGKTALN QAILQLGGFT VNNWTEECTH LVMVSVKVTI K TICALICG ...String:
MWKLLPAAGP AGGEPYRLLT GVEYVVGRKN CAILIENDQS ISRNHAVLTA NFSVTNLSQT DEIPVLTLKD NSKYGTFVNE EKMQNGFSR TLKSGDGITF GVFGSKFRIE YEPLVACSSC LDVSGKTALN QAILQLGGFT VNNWTEECTH LVMVSVKVTI K TICALICG RPIVKPEYFT EFLKAVESKK QPPQIESFYP PLDEPSIGSK NVDLSGRQER KQIFKGKTFI FLNAKQHKKL SS AVVFGGG EARLITEENE EEHNFFLAPG TCVVDTGITN SQTLIPDCQK KWIQSIMDML QRQGLRPIPE AEIGLAVIFM TTK NYCDPQ GHPSTGLKTT TPGPSLSQGV SVDEKLMPSA PVNTTTYVAD TESEQADTWD LSERPKEIKV SKMEQKFRML SQDA PTVKE SCKTSSNNNS MVSNTLAKMR IPNYQLSPTK LPSINKSKDR ASQQQQTNSI RNYFQPSTKK RERDEENQEM SSCKS ARIE TSCSLLEQTQ PATPSLWKNK EQHLSENEPV DTNSDNNLFT DTDLKSIVKN SASKSHAAEK LRSNKKREMD DVAIED EVL EQLFKDTKPE LEIDVKVQKQ EEDVNVRKRP RMDIETNDTF SDEAVPESSK ISQENEIGKK RELKEDSLWS AKEISNN DK LQDDSEMLPK KLLLTEFRSL VIKNSTSRNP SGINDDYGQL KNFKKFKKVT YPGAGKLPHI IGGSDLIAHH ARKNTELE E WLRQEMEVQN QHAKEESLAD DLFRYNPYLK RRR

UniProtKB: Nibrin

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Macromolecule #4: DNA repair protein RAD50

MacromoleculeName: DNA repair protein RAD50 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 154.150016 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG TKGNTFVHDP KVAQETDVRA QIRLQFRDV NGELIAVQRS MVCTQKSKKT EFKTLEGVIT RTKHGEKVSL SSKCAEIDRE MISSLGVSKA VLNNVIFCHQ E DSNWPLSE ...String:
MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG TKGNTFVHDP KVAQETDVRA QIRLQFRDV NGELIAVQRS MVCTQKSKKT EFKTLEGVIT RTKHGEKVSL SSKCAEIDRE MISSLGVSKA VLNNVIFCHQ E DSNWPLSE GKALKQKFDE IFSATRYIKA LETLRQVRQT QGQKVKEYQM ELKYLKQYKE KACEIRDQIT SKEAQLTSSK EI VKSYENE LDPLKNRLKE IEHNLSKIMK LDNEIKALDS RKKQMEKDNS ELEEKMEKVF QGTDEQLNDL YHNHQRTVRE KER KLVDCH RELEKLNKES RLLNQEKSEL LVEQGRLQLQ ADRHQEHIRA RDSLIQSLAT QLELDGFERG PFSERQIKNF HKLV RERQE GEAKTANQLM NDFAEKETLK QKQIDEIRDK KTGLGRIIEL KSEILSKKQN ELKNVKYELQ QLEGSSDRIL ELDQE LIKA ERELSKAEKN SNVETLKMEV ISLQNEKADL DRTLRKLDQE MEQLNHHTTT RTQMEMLTKD KADKDEQIRK IKSRHS DEL TSLLGYFPNK KQLEDWLHSK SKEINQTRDR LAKLNKELAS SEQNKNHINN ELKRKEEQLS SYEDKLFDVC GSQDFES DL DRLKEEIEKS SKQRAMLAGA TAVYSQFITQ LTDENQSCCP VCQRVFQTEA ELQEVISDLQ SKLRLAPDKL KSTESELK K KEKRRDEMLG LVPMRQSIID LKEKEIPELR NKLQNVNRDI QRLKNDIEEQ ETLLGTIMPE EESAKVCLTD VTIMERFQM ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD TVSSKIELNR KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEE QTVELSTEVQ SLYREIKDAK EQVSPLETTL EKFQQEKEEL INKKNTSNKI AQDKLNDIKE KVKNIHGYMK D IENYIQDG KDDYKKQKET ELNKVIAQLS ECEKHKEKIN EDMRLMRQDI DTQKIQERWL QDNLTLRKRN EELKEVEEER KQ HLKEMGQ MQVLQMKSEH QKLEENIDNI KRNHNLALGR QKGYEEEIIH FKKELREPQF RDAEEKYREM MIVMRTTELV NKD LDIYYK TLDQAIMKFH SMKMEEINKI IRDLWRSTYR GQDIEYIEIR SDADENVSAS DKRRNYNYRV VMLKGDTALD MRGR CSAGQ KVLASLIIRL ALAETFCLNC GIIALDEPTT NLDRENIESL AHALVEIIKS RSQQRNFQLL VITHDEDFVE LLGRS EYVE KFYRIKKNID QCSEIVKCSV SSLGFNVH

UniProtKB: DNA repair protein RAD50

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Macromolecule #5: Double-strand break repair protein MRE11

MacromoleculeName: Double-strand break repair protein MRE11 / type: protein_or_peptide / ID: 5
Details: His129 was mutated to Asn for nuclease-dead variant. Following residue R708 is a short GS linker, a PreScission cleavage site, and two FLAG tags.
Number of copies: 2 / Enantiomer: LEVO / EC number: Hydrolases; Acting on ester bonds
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 84.008633 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSTADALDDE NTFKILVATD IHLGFMEKDA VRGNDTFVTL DEILRLAQEN EVDFILLGGD LFHENKPSRK TLHTCLELLR KYCMGDRPV QFEILSDQSV NFGFSKFPWV NYQDGNLNIS IPVFSIHGNN DDPTGADALC ALDILSCAGF VNHFGRSMSV E KIDISPVL ...String:
MSTADALDDE NTFKILVATD IHLGFMEKDA VRGNDTFVTL DEILRLAQEN EVDFILLGGD LFHENKPSRK TLHTCLELLR KYCMGDRPV QFEILSDQSV NFGFSKFPWV NYQDGNLNIS IPVFSIHGNN DDPTGADALC ALDILSCAGF VNHFGRSMSV E KIDISPVL LQKGSTKIAL YGLGSIPDER LYRMFVNKKV TMLRPKEDEN SWFNLFVIHQ NRSKHGSTNF IPEQFLDDFI DL VIWGHEH ECKIAPTKNE QQLFYISQPG SSVVTSLSPG EAVKKHVGLL RIKGRKMNMH KIPLHTVRQF FMEDIVLANH PDI FNPDNP KVTQAIQSFC LEKIEEMLEN AERERLGNSH QPEKPLVRLR VDYSGGFEPF SVLRFSQKFV DRVANPKDII HFFR HREQK EKTGEEINFG KLITKPSEGT TLRVEDLVKQ YFQTAEKNVQ LSLLTERGMG EAVQEFVDKE EKDAIEELVK YQLEK TQRF LKERHIDALE DKIDEEVRRF RETRQKNTNE EDDEVREAMT RARALRSQSE ESASAFSADD LMSIDLAEQM ANDSDD SIS AATNKGRGRG RGRRGGRGQN SASRGGSQRG RADTGLETST RSRNSKTAVS ASRNMSIIDA FKSTRQQPSR NVTTKNY SE VIEVDESDVE EDIFPTTSKT DQRWSSTSSS KIMSQSQVSK GVDFESSEDD DDDPFMNTSS LRRNRRSGGS LEVLFQGP D YKDDDDKGTD YKDDDDK

UniProtKB: Double-strand break repair protein MRE11

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Macromolecule #6: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #7: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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Macromolecule #8: BERYLLIUM TRIFLUORIDE ION

MacromoleculeName: BERYLLIUM TRIFLUORIDE ION / type: ligand / ID: 8 / Number of copies: 2 / Formula: BEF
Molecular weightTheoretical: 66.007 Da
Chemical component information

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

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Macromolecule #9: MANGANESE (II) ION

MacromoleculeName: MANGANESE (II) ION / type: ligand / ID: 9 / Number of copies: 2 / Formula: MN
Molecular weightTheoretical: 54.938 Da

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Macromolecule #10: water

MacromoleculeName: water / type: ligand / ID: 10 / Number of copies: 4 / 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: 7.5
Details: 25mM Hepes-NaOH, pH 7.5, 150 mM NaCl, 1 mM DTT, 1 mM ATP, 1mM BeF3, 5 mM MgCl2, 1 mM MnCl2
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 12 sec. / Details: 20 mA, 12 s
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 283 K / Instrument: LEICA PLUNGER

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Detector mode: COUNTING / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.6 µm / Nominal defocus min: 0.5 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC (ver. 4.6.2) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.79 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.6.2) / Number images used: 172784
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.6.2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.6.2)
Final 3D classificationNumber classes: 3 / Software - Name: cryoSPARC (ver. 4.6.2)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9q9i:
Cryo-EM structure of human Mre11-Rad50-Nbs1 complex bound to DNA

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