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- EMDB-26140: ATP and DNA bound SMC5/6 core complex -

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Basic information

Entry
Database: EMDB / ID: EMD-26140
TitleATP and DNA bound SMC5/6 core complex
Map dataPrimary map
Sample
  • Complex: Hexamer complex of Smc5-Smc6-Nse1-Nse3-Nse4-Nse2 with ATP and DNA
    • DNA: DNA (68-MER)
    • DNA: DNA (78-MER)
    • Protein or peptide: Non-structural maintenance of chromosomes element 1
    • Protein or peptide: Structural maintenance of chromosomes protein 6
    • Protein or peptide: Structural maintenance of chromosomes protein 5
    • Protein or peptide: Non-structural maintenance of chromosome element 3
    • Protein or peptide: Non-structural maintenance of chromosome element 4
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
KeywordsNse1 / Nse3 / Nse4 / Smc5 / Smc6 / Nse2 / ATP / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


Smc5-Smc6 complex / resolution of DNA recombination intermediates / DNA double-strand break attachment to nuclear envelope / chromosome separation / SUMOylation of DNA damage response and repair proteins / Platelet degranulation / chromatin looping / recombinational repair / regulation of telomere maintenance / protein sumoylation ...Smc5-Smc6 complex / resolution of DNA recombination intermediates / DNA double-strand break attachment to nuclear envelope / chromosome separation / SUMOylation of DNA damage response and repair proteins / Platelet degranulation / chromatin looping / recombinational repair / regulation of telomere maintenance / protein sumoylation / double-strand break repair via homologous recombination / site of double-strand break / single-stranded DNA binding / damaged DNA binding / chromosome, telomeric region / DNA repair / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / mitochondrion / ATP binding / nucleus / cytoplasm
Similarity search - Function
Non-structural maintenance of chromosome element 4, C-terminal / Nse4/EID family / Nse4/EID protein, Nse3/MAGE-binding domain / Nse4 C-terminal / Binding domain of Nse4/EID3 to Nse3-MAGE / Structural maintenance of chromosomes protein 5 / MAGE homology domain / Melanoma-associated antigen / MAGE homology domain, winged helix WH1 motif / MAGE homology domain, winged helix WH2 motif ...Non-structural maintenance of chromosome element 4, C-terminal / Nse4/EID family / Nse4/EID protein, Nse3/MAGE-binding domain / Nse4 C-terminal / Binding domain of Nse4/EID3 to Nse3-MAGE / Structural maintenance of chromosomes protein 5 / MAGE homology domain / Melanoma-associated antigen / MAGE homology domain, winged helix WH1 motif / MAGE homology domain, winged helix WH2 motif / MAGE homology domain / Melanoma-associated antigen / Rad50/SbcC-type AAA domain / AAA domain / RecF/RecN/SMC, N-terminal / RecF/RecN/SMC N terminal domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
: / Non-structural maintenance of chromosome element 4 / Non-structural maintenance of chromosome element 3 / Structural maintenance of chromosomes protein 5 / Structural maintenance of chromosomes protein 6
Similarity search - Component
Biological speciesSaccharomyces cerevisiae W303 (yeast) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsYu Y / Patel DJ
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM080670 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM131058 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2022
Title: Cryo-EM structure of DNA-bound Smc5/6 reveals DNA clamping enabled by multi-subunit conformational changes.
Authors: You Yu / Shibai Li / Zheng Ser / Huihui Kuang / Thane Than / Danying Guan / Xiaolan Zhao / Dinshaw J Patel /
Abstract: Structural maintenance of chromosomes (SMC) complexes are essential for chromatin organization and functions throughout the cell cycle. The cohesin and condensin SMCs fold and tether DNA, while ...Structural maintenance of chromosomes (SMC) complexes are essential for chromatin organization and functions throughout the cell cycle. The cohesin and condensin SMCs fold and tether DNA, while Smc5/6 directly promotes DNA replication and repair. The functions of SMCs rely on their abilities to engage DNA, but how Smc5/6 binds and translocates on DNA remains largely unknown. Here, we present a 3.8 Å cryogenic electron microscopy (cryo-EM) structure of DNA-bound Saccharomyces cerevisiae Smc5/6 complex containing five of its core subunits, including Smc5, Smc6, and the Nse1-3-4 subcomplex. Intricate interactions among these subunits support the formation of a clamp that encircles the DNA double helix. The positively charged inner surface of the clamp contacts DNA in a nonsequence-specific manner involving numerous DNA binding residues from four subunits. The DNA duplex is held up by Smc5 and 6 head regions and positioned between their coiled-coil arm regions, reflecting an engaged-head and open-arm configuration. The Nse3 subunit secures the DNA from above, while the hook-shaped Nse4 kleisin forms a scaffold connecting DNA and all other subunits. The Smc5/6 DNA clamp shares similarities with DNA-clamps formed by other SMCs but also exhibits differences that reflect its unique functions. Mapping cross-linking mass spectrometry data derived from DNA-free Smc5/6 to the DNA-bound Smc5/6 structure identifies multi-subunit conformational changes that enable DNA capture. Finally, mutational data from cells reveal distinct DNA binding contributions from each subunit to Smc5/6 chromatin association and cell fitness. In summary, our integrative study illuminates how a unique SMC complex engages DNA in supporting genome regulation.
History
DepositionFeb 4, 2022-
Header (metadata) releaseJun 22, 2022-
Map releaseJun 22, 2022-
UpdateFeb 21, 2024-
Current statusFeb 21, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_26140.png

Downloads & links

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Map

FileDownload / File: emd_26140.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPrimary map
Voxel sizeX=Y=Z: 1.069 Å
Density
Contour LevelBy AUTHOR: 0.012
Minimum - Maximum-0.08608429 - 0.1549636
Average (Standard dev.)0.00012464153 (±0.0020352425)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 320.7 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Hexamer complex of Smc5-Smc6-Nse1-Nse3-Nse4-Nse2 with ATP and DNA

EntireName: Hexamer complex of Smc5-Smc6-Nse1-Nse3-Nse4-Nse2 with ATP and DNA
Components
  • Complex: Hexamer complex of Smc5-Smc6-Nse1-Nse3-Nse4-Nse2 with ATP and DNA
    • DNA: DNA (68-MER)
    • DNA: DNA (78-MER)
    • Protein or peptide: Non-structural maintenance of chromosomes element 1
    • Protein or peptide: Structural maintenance of chromosomes protein 6
    • Protein or peptide: Structural maintenance of chromosomes protein 5
    • Protein or peptide: Non-structural maintenance of chromosome element 3
    • Protein or peptide: Non-structural maintenance of chromosome element 4
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: Hexamer complex of Smc5-Smc6-Nse1-Nse3-Nse4-Nse2 with ATP and DNA

SupramoleculeName: Hexamer complex of Smc5-Smc6-Nse1-Nse3-Nse4-Nse2 with ATP and DNA
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7 / Details: Smc5 E1015Q mutation and Smc6 E1048Q mutation
Source (natural)Organism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightTheoretical: 410 KDa

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Macromolecule #1: DNA (68-MER)

MacromoleculeName: DNA (68-MER) / type: dna / ID: 1 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 21.253111 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) ...String:
(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)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)

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Macromolecule #2: DNA (78-MER)

MacromoleculeName: DNA (78-MER) / type: dna / ID: 2 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 23.682055 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) ...String:
(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)(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 #3: Non-structural maintenance of chromosomes element 1

MacromoleculeName: Non-structural maintenance of chromosomes element 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightTheoretical: 38.437395 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MEVHEEHVSA PVTGDATAKY LLQYILSARG ICHENALILA LMRLETDAST LNTEWSIQQW VDKLNDYINA INVKLNLLGY KIIRINHGI GRNAVTLKAK QNFESFEDNT AIRAHDNDYA VLQSIVLPES NRFFVYVNLA STEETKLATR FNQNEIEFIK W AIEQFMIS ...String:
MEVHEEHVSA PVTGDATAKY LLQYILSARG ICHENALILA LMRLETDAST LNTEWSIQQW VDKLNDYINA INVKLNLLGY KIIRINHGI GRNAVTLKAK QNFESFEDNT AIRAHDNDYA VLQSIVLPES NRFFVYVNLA STEETKLATR FNQNEIEFIK W AIEQFMIS GETIVEGPAL DTSIIVREVN RILVAATGDS NLAKWRKFST FTVGSTNLFQ FQELTATDIE DLLLRLCELK WF YRTQEGK FGIDLRCIAE LEEYLTSMYN LNTCQNCHKL AIQGVRCGNE SCREENEETG ENSLSQIWHV DCFKHYITHV SKN CDRCGS SLITEGVYVI G

UniProtKB: UNIPROTKB: A0A7I9FFW3

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Macromolecule #4: Structural maintenance of chromosomes protein 6

MacromoleculeName: Structural maintenance of chromosomes protein 6 / type: protein_or_peptide / ID: 4 / Details: Smc6(E1048Q)-2XStrep / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightTheoretical: 132.445078 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MISTTISGKR PIEQVDDELL SLTAQQENEE QQQQRKRRRH QFAPMTQFNS NTLDEDSGFR SSSDVATADQ DNFLEESPSG YIKKVILRN FMCHEHFELE LGSRLNFIVG NNGSGKSAIL TAITIGLGAK ASETNRGSSL KDLIREGCYS AKIILHLDNS K YGAYQQGI ...String:
MISTTISGKR PIEQVDDELL SLTAQQENEE QQQQRKRRRH QFAPMTQFNS NTLDEDSGFR SSSDVATADQ DNFLEESPSG YIKKVILRN FMCHEHFELE LGSRLNFIVG NNGSGKSAIL TAITIGLGAK ASETNRGSSL KDLIREGCYS AKIILHLDNS K YGAYQQGI FGNEIIVERI IKRDGPASFS LRSENGKEIS NKKKDIQTVV DYFSVPVSNP MCFLSQDAAR SFLTASTSQD KY SHFMKGT LLQEITENLL YASAIHDSAQ ENMALHLENL KSLKAEYEDA KKLLRELNQT SDLNERKMLL QAKSLWIDVA HNT DACKNL ENEISGIQQK VDEVTEKIRN RQEKIERYTS DGTTIEAQID AKVIYVNEKD SEHQNARELL RDVKSRFEKE KSNQ AEAQS NIDQGRKKVD ALNKTIAHLE EELTKEMGGD KDQMRQELEQ LEKANEKLRE VNNSLVVSLQ DVKNEERDIQ HERES ELRT ISRSIQNKKV ELQNIAKGND TFLMNFDRNM DRLLRTIEQR KNEFETPAIG PLGSLVTIRK GFEKWTRSIQ RAISSS LNA FVVSNPKDNR LFRDIMRSCG IRSNIPIVTY CLSQFDYSKG RAHGNYPTIV DALEFSKPEI ECLFVDLSRI ERIVLIE DK NEARNFLQRN PVNVNMALSL RDRRSGFQLS GGYRLDTVTY QDKIRLKVNS SSDNGTQYLK DLIEQETKEL QNIRDRYE E KLSEVRSRLK EIDGRLKSTK NEMRKTNFRM TELKMNVGKV VDTGILNSKI NERKNQEQAI ASYEAAKEEL GLKIEQIAQ EAQPIKEQYD STKLALVEAQ DELQQLKEDI NSRQSKIQKY KDDTIYYEDK KKVYLENIKK IEVNVAALKE GIQRQIQNAC AFCSKERIE NVDLPDTQEE IKRELDKVSR MIQKAEKSLG LSQEEVIALF EKCRNKYKEG QKKYMEIDEA LNRLHNSLKA R DQNYKNAE KGTCFDADMD FRASLKVRKF SGNLSFIKDT KSLEIYILTT NDEKARNVDT LSGGEKSFSQ MALLLATWKP MR SRIIALD QFDVFMDQVN RKIGTTLIVK KLKDIARTQT IIITPQDIGK IADIDSSGVS IHRMRDPERQ NNSNFYNGSL EVL FQGPGG SSAWSHPQFE KGGGSGGGSG GGSWSHPQFE K

UniProtKB: Structural maintenance of chromosomes protein 6

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Macromolecule #5: Structural maintenance of chromosomes protein 5

MacromoleculeName: Structural maintenance of chromosomes protein 5 / type: protein_or_peptide / ID: 5 / Details: Smc5 (E1015Q) / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightTheoretical: 126.293234 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MTSLIDLGRY VERTHHGEDT EPRSKRVKIA KPDLSSFQPG SIIKIRLQDF VTYTLTEFNL SPSLNMIIGP NGSGKSTFVC AVCLGLAGK PEYIGRSKKV EDFIKNGQDV SKIEITLKNS PNVTDIEYID ARDETIKITR IITRSKRRSD YLINDYQVSE S VVKTLVAQ ...String:
MTSLIDLGRY VERTHHGEDT EPRSKRVKIA KPDLSSFQPG SIIKIRLQDF VTYTLTEFNL SPSLNMIIGP NGSGKSTFVC AVCLGLAGK PEYIGRSKKV EDFIKNGQDV SKIEITLKNS PNVTDIEYID ARDETIKITR IITRSKRRSD YLINDYQVSE S VVKTLVAQ LNIQLDNLCQ FLSQERVEEF ARLKSVKLLV ETIRSIDASL LDVLDELREL QGNEQSLQKD LDFKKAKIVH LR QESDKLR KSVESLRDFQ NKKGEIELHS QLLPYVKVKD HKEKLNIYKE EYERAKANLR AILKDKKPFA NTKKTLENQV EEL TEKCSL KTDEFLKAKE KINEIFEKLN TIRDEVIKKK NQNEYYRGRT KKLQATIIST KEDFLRSQEI LAQTHLPEKS VFED IDIKR KEIINKEGEI RDLISEIDAK ANAINHEMRS IQRQAESKTK SLTTTDKIGI LNQDQDLKEV RDAVLMVREH PEMKD KILE PPIMTVSAIN AQFAAYLAQC VDYNTSKALT VVDSDSYKLF ANPILDKFKV NLRELSSADT TPPVPAETVR DLGFEG YLS DFITGDKRVM KMLCQTSKIH TIPVSRRELT PAQIKKLITP RPNGKILFKR IIHGNRLVDI KQSAYGSKQV FPTDVSI KQ TNFYQGSIMS NEQKIRIENE IINLKNEYND RKSTLDALSN QKSGYRHELS ELASKNDDIN REAHQLNEIR KKYTMRKS T IETLREKLDQ LKREARKDVS QKIKDIDDQI QQLLLKQRHL LSKMASSMKS LKNCQKELIS TQILQFEAQN MDVSMNDVI GFFNEREADL KSQYEDKKKF VKEMRDTPEF QSWMREIRSY DQDTKEKLNK VAEKYEEEGN FNLSFVQDVL DKLESEIAMV NHDESAVTI LDQVTAELRE LEHTVPQQSK DLETIKAKLK EDHAVLEPKL DDIVSKISAR FARLFNNVGS AGAVRLEKPK D YAEWKIEI MVKFRDNAPL KKLDSHTQSG GERAVSTVLY MIALQEFTSA PFRVVDQINQ GMDSRNERIV HKAMVENACA EN TSQYFLI TPKLLTGLHY HEKMRIHCVM AGSWIPNPSE DPKMIHFGET SNYSFDG

UniProtKB: Structural maintenance of chromosomes protein 5

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Macromolecule #6: Non-structural maintenance of chromosome element 3

MacromoleculeName: Non-structural maintenance of chromosome element 3 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightTheoretical: 34.193777 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MMSSIDNDSD VDLTEDLAVA KIVKENPVAR KMVRYILSRG ESQNSIITRN KLQSVIHEAA REENIAKPSF SKMFMDINAI LYNVYGFEL QGLPSKNNMN AGGNGSNSNT NKSMPEPLGH RAQKFILLNN VPHSKNFDDF KILQSAHTYE ELIVTGEYIG D DIASGTSN ...String:
MMSSIDNDSD VDLTEDLAVA KIVKENPVAR KMVRYILSRG ESQNSIITRN KLQSVIHEAA REENIAKPSF SKMFMDINAI LYNVYGFEL QGLPSKNNMN AGGNGSNSNT NKSMPEPLGH RAQKFILLNN VPHSKNFDDF KILQSAHTYE ELIVTGEYIG D DIASGTSN TLESKLSTDR DLVYKGVLSV ILCIVFFSKN NILHQELIKF LETFGIPSDG SKIAILNITI EDLIKSLEKR EY IVRLEEK SDTDGEVISY RIGRRTQAEL GLESLEKLVQ EIMGLEKEQT KSLHDDIIKS IGDSYSIG

UniProtKB: Non-structural maintenance of chromosome element 3

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Macromolecule #7: Non-structural maintenance of chromosome element 4

MacromoleculeName: Non-structural maintenance of chromosome element 4 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightTheoretical: 46.252996 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MSSTVISRKR RNSTVTEPDS SGETRKQKKS RSDEKSSSSK DGDPQLEFKV LQGYRDLESE MHKGRAQVTR TGDIGVAMDN LNAVDSLFN KVIGIKNNGL FAHDARAMVS ISELAQISVR NLKFDDSRSM VNLENIVNSL KRYMLKEHFK LNNIAENRND L TLAADEQS ...String:
MSSTVISRKR RNSTVTEPDS SGETRKQKKS RSDEKSSSSK DGDPQLEFKV LQGYRDLESE MHKGRAQVTR TGDIGVAMDN LNAVDSLFN KVIGIKNNGL FAHDARAMVS ISELAQISVR NLKFDDSRSM VNLENIVNSL KRYMLKEHFK LNNIAENRND L TLAADEQS AADQQEESDG DIDRTPDDNH TDKATSSFKA TSMRHSYLQQ FSHYNEFSQF NWFRIGALYN TISKNAPITD HL MGPLSIE KKPRVLTQRR RNNDQVGEKI TAEKITQHSL NSTQQETTPE QVKKCFKKLS KKLGPEGSIN LFKFIIDPNS FSR SIENLF YTSFLIKEGK LLMEHDEEGL PTIKIKQSIS HTDSRSKEIE RQRRRAAHQN HIIFQMDMPT WRKLIKKYNI TSPF LDG

UniProtKB: Non-structural maintenance of chromosome element 4

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Macromolecule #8: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 8 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

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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

Concentration0.3 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 53.55 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL / In silico model: AlphaFold
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final 3D classificationNumber classes: 4 / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 201249

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