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- EMDB-13783: Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (... -

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Basic information

Entry
Database: EMDB / ID: EMD-13783
TitleCryo-EM structure of clamped S.cerevisiae condensin-DNA complex (Form I)
Map data
Sample
  • Complex: complex of condensin tetramer (smc2, smc4, brn1, ycs4), DNA, ADP-BeF3
    • Protein or peptide: Structural maintenance of chromosomes protein 2
    • Protein or peptide: Structural maintenance of chromosomes protein 4
    • Protein or peptide: Condensin complex subunit 2
    • Protein or peptide: Condensin complex subunit 1
    • DNA: DNA (36-MER)
    • DNA: DNA (36-MER)
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: BERYLLIUM TRIFLUORIDE ION
  • Ligand: MAGNESIUM ION
Function / homology
Function and homology information


negative regulation of meiotic DNA double-strand break formation / meiotic chromosome condensation / Condensation of Prometaphase Chromosomes / tRNA gene clustering / meiotic chromosome separation / condensin complex / DNA secondary structure binding / maintenance of rDNA / rDNA chromatin condensation / synaptonemal complex assembly ...negative regulation of meiotic DNA double-strand break formation / meiotic chromosome condensation / Condensation of Prometaphase Chromosomes / tRNA gene clustering / meiotic chromosome separation / condensin complex / DNA secondary structure binding / maintenance of rDNA / rDNA chromatin condensation / synaptonemal complex assembly / nucleophagy / condensed chromosome, centromeric region / mitotic chromosome condensation / chromosome condensation / silent mating-type cassette heterochromatin formation / minor groove of adenine-thymine-rich DNA binding / mitotic sister chromatid segregation / condensed chromosome / histone binding / double-stranded DNA binding / cell division / chromatin binding / chromatin / nucleolus / ATP hydrolysis activity / mitochondrion / ATP binding / nucleus / cytoplasm
Similarity search - Function
Condensin subunit 1 / Condensin complex subunit 1, N-terminal / Condensin subunit 1/Condensin-2 complex subunit D3 / Condensin complex subunit 1, C-terminal / non-SMC mitotic condensation complex subunit 1, N-term / non-SMC mitotic condensation complex subunit 1 / Smc2, ATP-binding cassette domain / Condensin complex subunit 2/barren / Condensin complex subunit 2 / Structural maintenance of chromosomes protein ...Condensin subunit 1 / Condensin complex subunit 1, N-terminal / Condensin subunit 1/Condensin-2 complex subunit D3 / Condensin complex subunit 1, C-terminal / non-SMC mitotic condensation complex subunit 1, N-term / non-SMC mitotic condensation complex subunit 1 / Smc2, ATP-binding cassette domain / Condensin complex subunit 2/barren / Condensin complex subunit 2 / Structural maintenance of chromosomes protein / SMCs flexible hinge / SMCs flexible hinge superfamily / SMC proteins Flexible Hinge Domain / SMC proteins Flexible Hinge Domain / RecF/RecN/SMC, N-terminal / RecF/RecN/SMC N terminal domain / Armadillo-like helical / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Condensin complex subunit 2 / Structural maintenance of chromosomes protein 2 / Condensin complex subunit 1 / Structural maintenance of chromosomes protein 4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288C (yeast) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsLee B-G / Rhodes J / Lowe J
Funding support United Kingdom, 3 items
OrganizationGrant numberCountry
Wellcome Trust218621/Z/19/Z United Kingdom
Wellcome Trust202754/Z/16/Z United Kingdom
Medical Research Council (MRC, United Kingdom)U105184326 United Kingdom
CitationJournal: Proc Natl Acad Sci U S A / Year: 2022
Title: Clamping of DNA shuts the condensin neck gate.
Authors: Byung-Gil Lee / James Rhodes / Jan Löwe /
Abstract: SignificanceDNA needs to be compacted to fit into nuclei and during cell division, when dense chromatids are formed for their mechanical segregation, a process that depends on the protein complex ...SignificanceDNA needs to be compacted to fit into nuclei and during cell division, when dense chromatids are formed for their mechanical segregation, a process that depends on the protein complex condensin. It forms and enlarges loops in DNA through loop extrusion. Our work resolves the atomic structure of a DNA-bound state of condensin in which ATP has not been hydrolyzed. The DNA is clamped within a compartment that has been reported previously in other structural maintenance of chromosomes (SMC) complexes, including Rad50, cohesin, and MukBEF. With the caveat of important differences, it means that all SMC complexes cycle through at least some similar states and undergo similar conformational changes in their head modules, while hydrolyzing ATP and translocating DNA.
History
DepositionOct 26, 2021-
Header (metadata) releaseMar 23, 2022-
Map releaseMar 23, 2022-
UpdateApr 13, 2022-
Current statusApr 13, 2022Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_13783.png

Downloads & links

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Map

FileDownload / File: emd_13783.map.gz / Format: CCP4 / Size: 16.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 162 pix.
= 173.34 Å		1.07 Å/pix.
x 162 pix.
= 173.34 Å		1.07 Å/pix.
x 162 pix.
= 173.34 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.03270672 - 2.0688243
Average (Standard dev.)0.0069678035 (±0.058647737)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions162162162
Spacing162162162
CellA=B=C: 173.34001 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : complex of condensin tetramer (smc2, smc4, brn1, ycs4), DNA, ADP-BeF3

EntireName: complex of condensin tetramer (smc2, smc4, brn1, ycs4), DNA, ADP-BeF3
Components
  • Complex: complex of condensin tetramer (smc2, smc4, brn1, ycs4), DNA, ADP-BeF3
    • Protein or peptide: Structural maintenance of chromosomes protein 2
    • Protein or peptide: Structural maintenance of chromosomes protein 4
    • Protein or peptide: Condensin complex subunit 2
    • Protein or peptide: Condensin complex subunit 1
    • DNA: DNA (36-MER)
    • DNA: DNA (36-MER)
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: BERYLLIUM TRIFLUORIDE ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: complex of condensin tetramer (smc2, smc4, brn1, ycs4), DNA, ADP-BeF3

SupramoleculeName: complex of condensin tetramer (smc2, smc4, brn1, ycs4), DNA, ADP-BeF3
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Recombinant expressionOrganism: Saccharomyces cerevisiae W303 (yeast)
Molecular weightExperimental: 515 kDa/nm

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Macromolecule #1: Structural maintenance of chromosomes protein 2

MacromoleculeName: Structural maintenance of chromosomes protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 134.125875 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MKVEELIIDG FKSYATRTVI TDWDPQFNAI TGLNGSGKSN ILDAICFVLG IASMSTVRAS SLQDLIYKRG QAGVTKASVT IVFDNTDKS NSPIGFTNSP QISVTRQVVL GGTSKYLING HRAPQQSVLQ LFQSVQLNIN NPNFLIMQGK ITKVLNMKPS E ILSLIEEA ...String:
MKVEELIIDG FKSYATRTVI TDWDPQFNAI TGLNGSGKSN ILDAICFVLG IASMSTVRAS SLQDLIYKRG QAGVTKASVT IVFDNTDKS NSPIGFTNSP QISVTRQVVL GGTSKYLING HRAPQQSVLQ LFQSVQLNIN NPNFLIMQGK ITKVLNMKPS E ILSLIEEA AGTKMFEDRR EKAERTMSKK ETKLQENRTL LTEEIEPKLE KLRNEKRMFL EFQSTQTDLE KTERIVVSYE YY NIKHKHT SIRETLENGE TRMKMLNEFV KKTSEEIDSL NEDVEEIKLQ KEKELHKEGT ISKLENKENG LLNEISRLKT SLS IKVENL NDTTEKSKAL ESEIASSSAK LIEKKSAYAN TEKDYKMVQE QLSKQRDLYK RKEELVSTLT TGISSTGAAD GGYN AQLAK AKTELNEVSL AIKKSSMKME LLKKELLTIE PKLKEATKDN ELNVKHVKQC QETCDKLRAR LVEYGFDPSR IKDLK QRED KLKSHYYQTC KNSEYLKRRV TNLEFNYTKP YPNFEASFVH GVVGQLFQID NDNIRYATAL QTCAGGRLFN VVVQDS QTA TQLLERGRLR KRVTIIPLDK IYTRPISSQV LDLAKKIAPG KVELAINLIR FDESITKAME FIFGNSLICE DPETAKK IT FHPKIRARSI TLQGDVYDPE GTLSGGSRNT SESLLVDIQK YNQIQKQIET IQADLNHVTE ELQTQYATSQ KTKTIQSD L NLSLHKLDLA KRNLDANPSS QIIARNEEIL RDIGECENEI KTKQMSLKKC QEEVSTIEKD MKEYDSDKGS KLNELKKEL KLLAKELEEQ ESESERKYDL FQNLELETEQ LSSELDSNKT LLHNHLKSIE SLKLENSDLE GKIRGVEDDL VTVQTELNEE KKRLMDIDD ELNELETLIK KKQDEKKSSE LELQKLVHDL NKYKSNTNNM EKIIEDLRQK HEFLEDFDLV RNIVKQNEGI D LDTYRERS KQLNEKFQEL RKKVNPNIMN MIENVEKKEA ALKTMIKTIE KDKMKIQETI SKLNEYKRET LVKTWEKVTL DF GNIFADL LPNSFAKLVP CEGKDVTQGL EVKVKLGNIW KESLIELSGG QRSLIALSLI MALLQFRPAP MYILDEVDAA LDL SHTQNI GHLIKTRFKG SQFIVVSLKE GMFANANRVF RTRFQDGTSV VSIM

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Macromolecule #2: Structural maintenance of chromosomes protein 4

MacromoleculeName: Structural maintenance of chromosomes protein 4 / type: protein_or_peptide / ID: 2
Details: comment: since alignment with full sequence did not work, we input only sequence in pdb. The real sequence is UNIPROT Q12267 (full-length construct),comment: since alignment with full ...Details: comment: since alignment with full sequence did not work, we input only sequence in pdb. The real sequence is UNIPROT Q12267 (full-length construct),comment: since alignment with full sequence did not work, we input only sequence in pdb. The real sequence is UNIPROT Q12267 (full-length construct)
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 162.435812 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae W303 (yeast)
SequenceString: MSDSPLSKRQ KRKSAQEPEL SLDQGDAEED SQVENRVNLS ENTPEPDLPA LEASYSKSYT PRKLVLSSGE NRYAFSQPTN STTTSLHVP NLQPPKTSSR GRDHKSYSQS PPRSPGRSPT RRLELLQLSP VKNSRVELQK IYDRHQSSSK QQSRLFINEL V LENFKSYA ...String:
MSDSPLSKRQ KRKSAQEPEL SLDQGDAEED SQVENRVNLS ENTPEPDLPA LEASYSKSYT PRKLVLSSGE NRYAFSQPTN STTTSLHVP NLQPPKTSSR GRDHKSYSQS PPRSPGRSPT RRLELLQLSP VKNSRVELQK IYDRHQSSSK QQSRLFINEL V LENFKSYA GKQVVGPFHT SFSAVVGPNG SGKSNVIDSM LFVFGFRANK MRQDRLSDLI HKSEAFPSLQ SCSVAVHFQY VI DESSGTS RIDEEKPGLI ITRKAFKNNS SKYYINEKES SYTEVTKLLK NEGIDLDHKR FLILQGEVEN IAQMKPKAEK ESD DGLLEY LEDIIGTANY KPLIEERMGQ IENLNEVCLE KENRFEIVDR EKNSLESGKE TALEFLEKEK QLTLLRSKLF QFKL LQSNS KLASTLEKIS SSNKDLEDEK MKFQESLKKV DEIKAQRKEI KDRISSCSSK EKTLVLERRE LEGTRVSLEE RTKNL VSKM EKAEKTLKST KHSISEAENM LEELRGQQTE HETEIKDLTQ LLEKERSILD DIKLSLKDKT KNISAEIIRH EKELEP WDL QLQEKESQIQ LAESELSLLE ETQAKLKKNV ETLEEKILAK KTHKQELQDL ILDLKKKLNS LKDERSQGEK NFTSAHL KL KEMQKVLNAH RQRAMEARSS LSKAQNKSKV LTALSRLQKS GRINGFHGRL GDLGVIDDSF DVAISTACPR LDDVVVDT V ECAQHCIDYL RKNKLGYARF ILLDRLRQFN LQPISTPENV PRLFDLVKPK NPKFSNAFYS VLRDTLVAQN LKQANNVAY GKKRFRVVTV DGKLIDISGT MSGGGNHVAK GLMKLGTNQS DKVDDYTPEE VDKIERELSE RENNFRVASD TVHEMEEELK KLRDHEPDL ESQISKAEME ADSLASELTL AEQQVKEAEM AYVKAVSDKA QLNVVMKNLE RLRGEYNDLQ SETKTKKEKI K GLQDEIMK IGGIKLQMQN SKVESVCQKL DILVAKLKKV KSASKKSGGD VVKFQKLLQN SERDVELSSD ELKVIEEQLK HT KLALAEN DTNMNETLNL KVELKEQSEQ LKEQMEDMEE SINEFKSIEI EMKNKLEKLN SLLTYIKSEI TQQEKGLNEL SIR DVTHTL GMLDDNKMDS VKEDVKNNQE LDQEYRSCET QDESEIKDAE TSCDNYHPMN IDETSDEVSR GIPRLSEDEL RELD VELIE SKINELSYYV EETNVDIGVL EEYARRLAEF KRRKLDLNNA VQKRDEVKEQ LGILKKKRFD EFMAGFNIIS MTLKE MYQM ITMGGNAELE LVDSLDPFSE GVTFSVMPPK KSWRNITNLS GGEKTLSSLA LVFALHKYKP TPLYVMDEID AALDFR NVS IVANYIKERT KNAQFIVISL RNNMFELAQQ LVGVYKRDNR TKSTTIKNID ILNRT

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Macromolecule #3: Condensin complex subunit 2

MacromoleculeName: Condensin complex subunit 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 86.323297 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae W303 (yeast)
SequenceString: MTTQLRYENN DDDERVEYNL FTNRSTMMAN FEEWIKMATD NKINSRNSWN FALIDYFYDL DVLKDGENNI NFQKASATLD GCIKIYSSR VDSVTTETGK LLSGLAQRKT NGASNGDDSN GGNGEGLGGD SDEANIEIDP LTGMPISNDP DVNNTRRRVY N RVLETTLV ...String:
MTTQLRYENN DDDERVEYNL FTNRSTMMAN FEEWIKMATD NKINSRNSWN FALIDYFYDL DVLKDGENNI NFQKASATLD GCIKIYSSR VDSVTTETGK LLSGLAQRKT NGASNGDDSN GGNGEGLGGD SDEANIEIDP LTGMPISNDP DVNNTRRRVY N RVLETTLV EFETIKMKEL DQELIIDPLF KKALVDFDEG GAKSLLLNTL NIDNTARVIF DASIKDTQNV GQGKLQRKEE EL IERDSLV DDENEPSQSL ISTRNDSTVN DSVISAPSME DEILSLGMDF IKFDQIAVCE ISGSIEQLRN VVEDINQAKD FIE NVNNRF DNFLTEEELQ AAVPDNAEDD SDGFDMGMQQ ELCYPDENHD NTSHDEQDDD NVNSTTGSIF EKDLMAYFDE NLNR NWRGR EHWKVRNFKK ANLVNKESDL LEETRTTIGD TTDKNTTDDK SMDTKKKHKQ KKVLEIDFFK TDDSFEDKVF ASKGR TKID MPIKNRKNDT HYLLPDDFHF STDRITRLFI KPGQKMSLFS HRKHTRGDVS SGLFEKSTVS ANHSNNDIPT IADEHF WAD NYERKEQEEK EKEQSKEVGD VVGGALDNPF EDDMDGVDFN QAFEGTDDNE EASVKLDLQD DEDHKFPIRE NKVTYSR VS KKVDVRRLKK NVWRSINNLI QEHDSRKNRE QSSNDSETHT EDESTKELKF SDIIQGISKM YSDDTLKDIS TSFCFICL L HLANEHGLQI THTENYNDLI VNYEDLATTQ AAS

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Macromolecule #4: Condensin complex subunit 1

MacromoleculeName: Condensin complex subunit 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 133.116766 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae W303 (yeast)
SequenceString: MSGFSLSEYL TKFQTTDRES YPRLQDPSRE LNVIIDQLAV SPEQIDASPD SLEALIDLCH DFPHLTPKLQ TQLSYLISSS LSNLSKDIK ANLSSNVNFT EIGGLIPQWK RHLEEYGYLI QVLLTFLQDE LHKVSSQSTN LNRSAKNSKN DSANVELFKR D CNQMENLL ...String:
MSGFSLSEYL TKFQTTDRES YPRLQDPSRE LNVIIDQLAV SPEQIDASPD SLEALIDLCH DFPHLTPKLQ TQLSYLISSS LSNLSKDIK ANLSSNVNFT EIGGLIPQWK RHLEEYGYLI QVLLTFLQDE LHKVSSQSTN LNRSAKNSKN DSANVELFKR D CNQMENLL ESITKLLEIN LSKIFQTTPE KDLFIGLFTR PLFVLLEIEP VTKVSSLKMF IQRILAMCVK NHGQSSSIQS SL MTNLTYF LHLSVFNAEL LKLLNDEYNY PQLTEDILKE ISTRVFNAKD TTGPKAISNF LIKLSELSPG IMLRQMNLVI TLL NNSSIT LRCSVVEACG NIVAELAQDP QTMEHYKQQI AVLIELLEER FQDSNPYVRT KAIQGCSKIC DLSSKFNKSK AKFT SLAVR SLQDRSSLVR RNSVKLLSKL LLKHPFKAIH GSQLRLSEWE EYLKGSESQL NSTLKKVESQ ETLNDTIERS LIEEE VEQD EGQCRTELEG SFNKSAELSR IENEVENINA TNTSVLMKLK LMIVYYKDAI SFIKEIHKSI ELISNLLFSK NRNEVL ESM DFLVLADAFD IELSEFGIKK MLHLVWMKGT NDEGTSISVH LIECYKQLFL TAPDSCNMQE KAAHIAKNLI NLSIGAS IA DLASLEQLLG MMYEQKLIDQ HVINILWAIY NSASKASMQK EQNVNNRDSE KGFSKEQIHG SIIILGMLSL ADNEIALK G LESLLNIGLG AVGLKDLTLC RYSCLALERM VPKRSTIITK AINQELEDVA VKKLYAIIIN YTKDNEYYPM CEQALSALF TISSKPDILA TDLIREKTMM TFGKPEEEDS ILSLEQSSRV VSLSQLLFIV GQVAIKTLVY LEKCEAEFKK RKIEAETRNG KVKNQGADV TNTTQDNGGD KELEMIGGTN EDDFTDAIQF VKENELLFGE KSILGKFCPI VEEIVSNSSR FSDPMLQRTA T LCLEKLMC LSSKYCEKSL PLLITVMEKS PDPTIRSNAV LGLGDMAVCF NNLVDENTDY LYRRLHDENL MVQRTCLMTV TF LILAGQV KVKGQLGEMA KCLDNPDQGI SDMCRLFFTE LASKDNAIYN GFIDIFSNLS SDDLLGKESF KKIIKFLLTF IDK ERHQKQ LNEKLVGRLR KCETQKQWDD IAFVLNNLPY KNEDVTALLE QGFKVVSAKE

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Macromolecule #5: DNA (36-MER)

MacromoleculeName: DNA (36-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 11.230485 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)

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Macromolecule #6: DNA (36-MER)

MacromoleculeName: DNA (36-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 10.905983 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)

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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 / Adenosine diphosphate

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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: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 9 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 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

BufferpH: 7.5
GridModel: UltrAuFoil R2/2 / Material: GOLD / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 55.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: CTFFIND (ver. 4)
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION
Final reconstructionNumber classes used: 1 / Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 286294

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Atomic model buiding 1

Initial model
PDB IDChain

6yvu

chain_id: A

6yvu

chain_id: B

6yvu

chain_id: C

6yvu

chain_id: D

6zz6

chain_id: E

6zz6

chain_id: F
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-7q2x:
Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (Form I)

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