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Open data
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Basic information
Entry | ![]() | ||||||||||||
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Title | Cryo-EM map of Chaetomium thermophilum MRN (RBD & bridge) | ||||||||||||
![]() | MRN RBD & bridge. Ref 3D map. | ||||||||||||
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![]() | DNA repair / complex / ATPase / coiled-coils / HYDROLASE | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.92 Å | ||||||||||||
![]() | Stakyte K / Rotheneder M / Bartho JD / Lammens K / Hopfner KP | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions Authors: Rotheneder M / Stakyte K | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 31.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 22.2 KB 22.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.5 KB | Display | ![]() |
Images | ![]() | 60.8 KB | ||
Masks | ![]() | 64 MB | ![]() | |
Filedesc metadata | ![]() | 7 KB | ||
Others | ![]() ![]() ![]() | 60.8 MB 59.5 MB 59.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 739.3 KB | Display | ![]() |
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Full document | ![]() | 738.9 KB | Display | |
Data in XML | ![]() | 16.6 KB | Display | |
Data in CIF | ![]() | 21.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | MRN RBD & bridge. Ref 3D map. | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.059 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: MRN RBD & bridge. LAFTER.
File | emd_14876_additional_1.map | ||||||||||||
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Annotation | MRN RBD & bridge. LAFTER. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: MRN RBD & bridge. Half map B.
File | emd_14876_half_map_1.map | ||||||||||||
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Annotation | MRN RBD & bridge. Half map B. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: MRN RBD & bridge. Half map A.
File | emd_14876_half_map_2.map | ||||||||||||
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Annotation | MRN RBD & bridge. Half map A. | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Chaetomium thermophilum Mre11-Rad50-Nbs1 complex bound to ATPyS
Entire | Name: Chaetomium thermophilum Mre11-Rad50-Nbs1 complex bound to ATPyS |
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Components |
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-Supramolecule #1: Chaetomium thermophilum Mre11-Rad50-Nbs1 complex bound to ATPyS
Supramolecule | Name: Chaetomium thermophilum Mre11-Rad50-Nbs1 complex bound to ATPyS type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Double-strand break repair protein
Macromolecule | Name: Double-strand break repair protein / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: MPQTAGPDTI RILVSTDNHV GYEERDPIRK DDSWRTFDEI MQLARTKDVD MVLLGGDLFH DNKPSRKAMY QVMRSLRKNC LGMKPCELEF LSDPAEVFEG AFPHVNYYDP DINVSIPVFS IHGNHDDPSG DGHLCSLDLL QVAGLVNYFG RVPEADNIHV KPILLQKGKT ...String: MPQTAGPDTI RILVSTDNHV GYEERDPIRK DDSWRTFDEI MQLARTKDVD MVLLGGDLFH DNKPSRKAMY QVMRSLRKNC LGMKPCELEF LSDPAEVFEG AFPHVNYYDP DINVSIPVFS IHGNHDDPSG DGHLCSLDLL QVAGLVNYFG RVPEADNIHV KPILLQKGKT KLALYGMSNV RDERIHRTFR DNKVRFYRPS QQTGDWFNLL TLHQNHYAHT PTGYLSENML PDFLDLVIWG HEHECLIDPK KNPETGFHVM QPGSSIATSL VPGEAVPKHI AILSITGKSF EVEKIPLRTV RPFVIREITL ATDKRFKGLE KKQDNRQEVT KRLMQIVEEM IAEANEMWRS LHEDSQDDED EEQPLPLIRL KVEYSSPEGT KFEVENPQRF SNRFAGKVAN QNDVVHFYRK KTGTTRKPKE GKRELPEGIA EALEDSDSIS VDALVQEFFA QQSLKILPQA PFGDAVNQFV SKDDKHAVEM FVMDSLSSQV RGLLQLDDDK INEGLDSHIE DFRKVMEKNF LSGQQKQAQR RRRFKEKPEG WDSDLNGHWT LQPEAIEELS SSPEPAKEGG RVRPASRITV GDEDNLFEEE EFVQKTTAKR APTTRATRKT AAATRATTAT KASAPAKKSI AAPRGRKRAN PFQDSAEEEE DVIMDDDDDY KPAPPVKAPP PKPARETQTR GAPKTRQTTL NFSQAERPTR TTQKAIEISD DEISEDDAFE SMPARKSKRY |
-Macromolecule #2: DH domain-containing protein
Macromolecule | Name: DH domain-containing protein / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: MSKIEKLSIL GVRSFGPHHP ETIAFNTPLT LIVGYNGSGK TTVIECLKYA TTGELPPNST RNGAFIHDPD LVGEKEVRAQ VKLSFRSTIG ESYVVTRNIQ LLVQRNNKRT QKTLEGSLLL RNNGERTVIS TRVAELDKLV SEKLGVPPAI LDAVIFCHQD DSLWPMSEPA ...String: MSKIEKLSIL GVRSFGPHHP ETIAFNTPLT LIVGYNGSGK TTVIECLKYA TTGELPPNST RNGAFIHDPD LVGEKEVRAQ VKLSFRSTIG ESYVVTRNIQ LLVQRNNKRT QKTLEGSLLL RNNGERTVIS TRVAELDKLV SEKLGVPPAI LDAVIFCHQD DSLWPMSEPA ALKKRFDEIF EAQKYTKVIE NIRLLKKKKG DELKILKERE VQDKANKERA EKVDRLMAQL TREILEAREK CNELSKQMEE ESAKIKDKYE QANSFLKIMN DLQTKTEKLE YKKDAIVELR SRIEELPDPD EVLRNTLDEY EQTINRIVAD RDHKAAQFHD LQAELKSARD QHTAKAAEQG KHQSDKEKYE RQLVARERMI REAAERHEIR GYNGDLDDRR IAIFNERIQK ILNDKRRELE RLQRENQEEL DRKTAVIAER ESRKQSVIRD RKAAKDRIIS LGKDMASIQG ELSSIDIDEG TEEMLRAEMK ELQARIEAAK ADEQNANLDA QIKEVNEEIW KLESLSAKLA RELVECTRLA SERAQLDLRR KQLAERKREL EIMTNTWNEQ FSTLLGEGWR PETLERDFSD VLKQQQLLVG EHRKKKDATQ QELKQAEYQL SNARNLHNKL TNEMEACMRA VQTAMKEARD LDSAPPVDEY ITMLETDEKE LAEVETALKL YDELKKHYST IKDRALRFNK CYICDRDFTN QEAAKTRLLE KVAKRLGDEE KKELLEDQAA FMKSLDILRA VRVKYDTYQR LSSELPQLSR EIDSETNRRE DLVRRLEDQD LAFREADNKL QEMETLNKHV MKITQLLKDI SDAEKQVERS QQLSNIETRS ADEINEEQTT CAEQTRAAQA KLTKLTAEKQ RLKDLVRQLE VERLQLENKI SSAVQQLERK KRLQESIARH KEDQNQARNA VQEADEELER LEPEIAGARA ALDEARQACR AKEQKVAAER DAIAQTVSEL NMINSEIQEY LDRGGPSSLA ANQRAIANLE TQMANLEGEM RELTVQINKL NKEIDNSDAK KRNIADNLTY RKNLREKDAL EREIAELEAR NAQEDYDRLI KEAHYLEAHR SKLNADRERL MGMMSTKDEE FRRLNEEYEL DLKDAKAKYK ETHIKVETTK AAIEDLGRGM AAVDHAIMQY HSKMMEQINR TIAELWQSTY QGTDIDTIQI RSDVESTTSS DSGTRRNYNY RVSMVKGDTE MDMRGRCSAG QKVLASIIIR LALAESFCAN CGLIALDEPT TNLDSDNIRS LAESLHGIIK ARQAQGNLQL IVITHDEEFL KYMQCSDFCD DFYRVKRDEK QNSVIVRESI TRITE |
-Macromolecule #3: FHA domain-containing protein
Macromolecule | Name: FHA domain-containing protein / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: MWILESELFD GKRLWLRPGK TYLFGRTVAE AGQLTISDKT VSRKHLTIHI DNVPEGGGRN LRSRSNVIVE DLESKKGTLV NGVQIRGQKT TLTEDVNEIK LGLCPKTLKI RWHPIVLSFS FTSKELRADP WTNLRDSLEQ LDIKYSAEYE PTTTHVVSKK RNTSKGLQAL ...String: MWILESELFD GKRLWLRPGK TYLFGRTVAE AGQLTISDKT VSRKHLTIHI DNVPEGGGRN LRSRSNVIVE DLESKKGTLV NGVQIRGQKT TLTEDVNEIK LGLCPKTLKI RWHPIVLSFS FTSKELRADP WTNLRDSLEQ LDIKYSAEYE PTTTHVVSKK RNTSKGLQAL INGRYIVTDS FINAIVQATE IPEGEEGASS ALEQDFEANW PNPLDHLPPR GEEPGNHTTE TYAPDARRQE VFDGYTFIFY EKKQYDNLFP AISAGKGKAL LKEVVPNRTR VDEFVRYVKS VAGEKGLGSF EDGSEGKGVV VVRYTPKGED SAWYAEFFTK FAQQLDHRPI DQKEFLEAIL ACDASMLRRP LEAMSQPVSV SASVEPQSSE KVRPAVEDRK EVEQSAPKQL QPSAEVPATE ESAPAPHRRE RRTGRSRFKG FDFDDDDIII ETPQAQSSTQ VPALPQVPSA SQDSLFVSQR EPSLAPSEPM LEEEAPCNTR TTRQTHRKRV LSPLPEHDNS ALLDEIAPIT AAVKRRRIEA GQDPVPPLPE PEPEREDEDV EMVEESPPRK GKKGAATTAK GKGKKIKQED EENVLELARR RREEAEAAAA AERQRLAQLG DDDIDYAAIR RLHIIEEIEV RQPEPHGPNR TREQDIADGR WDPRWNGRKN FKRFRRQGET GVRMPVQSVI VPLEEVRTKE YGIGDDYWLE DEEGRVPRRP KETQTQERST IGSVRDGSGF AAAAASGKGK EKDKENEKEV GRPGSSAAAA KQRSKPAPRR TVLTLDSSDE DEDEPSPHAP GIDTISDSEP EVVSSFPSVI PASEPSRSRA AKAAERANAL RSSAHSSQSQ TQQHRESQLS TGSSKIQLTL APGSSSLSFS RSGTAAGRNE NGKRPFGSFV SGESTASGRG MSVESGSVRG ESASKRQKQG SSGGGSFLAT RRKDDGSEEE SEDDELKFRF GRRR |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.27 mg/mL |
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Buffer | pH: 7.6 |
Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 43.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |