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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM structure of SA2-SCC1 complex at 2.9 angstrom | |||||||||
Map data | Postprocessed map of SA2-SCC1 complex | |||||||||
Sample |
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Keywords | Separase / cell cycle / SCC1 / RAD21 / protease / chromosome segregation / Auto-cleavage / SA1/2 / cohesin | |||||||||
| Function / homology | Function and homology informationnegative regulation of mitotic metaphase/anaphase transition / Cohesin Loading onto Chromatin / meiotic cohesin complex / Establishment of Sister Chromatid Cohesion / establishment of meiotic sister chromatid cohesion / cohesin complex / mitotic cohesin complex / positive regulation of sister chromatid cohesion / negative regulation of glial cell apoptotic process / negative regulation of G2/M transition of mitotic cell cycle ...negative regulation of mitotic metaphase/anaphase transition / Cohesin Loading onto Chromatin / meiotic cohesin complex / Establishment of Sister Chromatid Cohesion / establishment of meiotic sister chromatid cohesion / cohesin complex / mitotic cohesin complex / positive regulation of sister chromatid cohesion / negative regulation of glial cell apoptotic process / negative regulation of G2/M transition of mitotic cell cycle / replication-born double-strand break repair via sister chromatid exchange / establishment of mitotic sister chromatid cohesion / chromatin looping / reciprocal meiotic recombination / sister chromatid cohesion / negative regulation of interleukin-1 beta production / mitotic spindle pole / lncRNA binding / positive regulation of interleukin-10 production / negative regulation of tumor necrosis factor production / chromosome, centromeric region / mitotic spindle assembly / SUMOylation of DNA damage response and repair proteins / cis-regulatory region sequence-specific DNA binding / protein localization to chromatin / Meiotic synapsis / Resolution of Sister Chromatid Cohesion / condensed nuclear chromosome / meiotic cell cycle / chromosome segregation / nuclear matrix / fibrillar center / spindle pole / Separation of Sister Chromatids / double-strand break repair / chromosome / midbody / DNA recombination / DNA-binding transcription factor binding / Estrogen-dependent gene expression / negative regulation of neuron apoptotic process / response to hypoxia / cell division / apoptotic process / chromatin binding / regulation of transcription by RNA polymerase II / chromatin / nucleolus / nucleoplasm / nucleus / membrane / cytosol Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Yu J / Schmidt S / Botto M / Boland A | |||||||||
| Funding support | Switzerland, 2 items
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Citation | Journal: To Be PublishedTitle: Structural insights into cohesin cleavage by human separase Authors: Yu J / Schmidt S / Botto M / Ghent CM / Morgan DO / Boland A | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_52298.map.gz | 162 MB | EMDB map data format | |
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| Header (meta data) | emd-52298-v30.xml emd-52298.xml | 34.1 KB 34.1 KB | Display Display | EMDB header |
| Images | emd_52298.png | 79.8 KB | ||
| Filedesc metadata | emd-52298.cif.gz | 7.8 KB | ||
| Others | emd_52298_additional_1.map.gz emd_52298_additional_2.map.gz emd_52298_additional_3.map.gz emd_52298_additional_4.map.gz emd_52298_half_map_1.map.gz emd_52298_half_map_2.map.gz | 122.7 MB 122.4 MB 122.4 MB 163.3 MB 226.3 MB 226.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-52298 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-52298 | HTTPS FTP |
-Validation report
| Summary document | emd_52298_validation.pdf.gz | 700.9 KB | Display | EMDB validaton report |
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| Full document | emd_52298_full_validation.pdf.gz | 700.5 KB | Display | |
| Data in XML | emd_52298_validation.xml.gz | 16.2 KB | Display | |
| Data in CIF | emd_52298_validation.cif.gz | 19.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52298 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52298 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9hmvMC ![]() 9hm7C ![]() 9hmaC ![]() 9hmsC ![]() 9hn0C ![]() 9hn4C ![]() 9hn5C C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_52298.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Postprocessed map of SA2-SCC1 complex | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.9024 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Unsharpened map of SA2-SCC1 complex
| File | emd_52298_additional_1.map | ||||||||||||
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| Annotation | Unsharpened map of SA2-SCC1 complex | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Additional map: Focus-refined map (mask 4) of SA2-SCC1 complex
| File | emd_52298_additional_2.map | ||||||||||||
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| Annotation | Focus-refined map (mask 4) of SA2-SCC1 complex | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Additional map: Focus-refined map (mask 3) of SA2-SCC1 complex
| File | emd_52298_additional_3.map | ||||||||||||
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| Annotation | Focus-refined map (mask 3) of SA2-SCC1 complex | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Additional map: Composite map (postprocessed) of SA2-SCC1 complex
| File | emd_52298_additional_4.map | ||||||||||||
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| Annotation | Composite map (postprocessed) of SA2-SCC1 complex | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map A of SA2-SCC1 complex
| File | emd_52298_half_map_1.map | ||||||||||||
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| Annotation | Half map A of SA2-SCC1 complex | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map B of SA2-SCC1 complex
| File | emd_52298_half_map_2.map | ||||||||||||
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| Annotation | Half map B of SA2-SCC1 complex | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : SA2-SCC1 complex
| Entire | Name: SA2-SCC1 complex |
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| Components |
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-Supramolecule #1: SA2-SCC1 complex
| Supramolecule | Name: SA2-SCC1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 130 KDa |
-Macromolecule #1: Cohesin subunit SA-2
| Macromolecule | Name: Cohesin subunit SA-2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 145.730422 KDa |
| Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
| Sequence | String: MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP AEKGKGGNGG GKPPSGPNRM NGHHQQNGVE NMMLFEVVK MGKSAMQSVV DDWIESYKHD RDIALLDLIN FFIQCSGCKG VVTAEMFRHM QNSEIIRKMT EEFDEDSGDY P LTMAGPQW ...String: MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP AEKGKGGNGG GKPPSGPNRM NGHHQQNGVE NMMLFEVVK MGKSAMQSVV DDWIESYKHD RDIALLDLIN FFIQCSGCKG VVTAEMFRHM QNSEIIRKMT EEFDEDSGDY P LTMAGPQW KKFKSSFCEF IGVLVRQCQY SIIYDEYMMD TVISLLTGLS DSQVRAFRHT STLAAMKLMT ALVNVALNLS IN MDNTQRQ YEAERNKMIG KRANERLELL LQKRKELQEN QDEIENMMNA IFKGVFVHRY RDAIAEIRAI CIEEIGIWMK MYS DAFLND SYLKYVGWTM HDKQGEVRLK CLTALQGLYY NKELNSKLEL FTSRFKDRIV SMTLDKEYDV AVQAIKLLTL VLQS SEEVL TAEDCENVYH LVYSAHRPVA VAAGEFLYKK LFSRRDPEED GMMKRRGRQG PNANLVKTLV FFFLESELHE HAAYL VDSM WDCATELLKD WECMNSLLLE EPLSGEEALT DRQESALIEI MLCTIRQAAE CHPPVGRGTG KRVLTAKEKK TQLDDR TKI TELFAVALPQ LLAKYSVDAE KVTNLLQLPQ YFDLEIYTTG RLEKHLDALL RQIRNIVEKH TDTDVLEACS KTYHALC NE EFTIFNRVDI SRSQLIDELA DKFNRLLEDF LQEGEEPDED DAYQVLSTLK RITAFHNAHD LSKWDLFACN YKLLKTGI E NGDMPEQIVI HALQCTHYVI LWQLAKITES SSTKEDLLRL KKQMRVFCQI CQHYLTNVNT TVKEQAFTIL CDILMIFSH QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD NNSADGQQED EASKIEALHK RRNLLAAFCK LIVYTVVEMN TAADIFKQY MKYYNDYGDI IKETMSKTRQ IDKIQCAKTL ILSLQQLFNE MIQENGYNFD RSSSTFSGIK ELARRFALTF G LDQLKTRE AIAMLHKDGI EFAFKEPNPQ GESHPPLNLA FLDILSEFSS KLLRQDKRTV YVYLEKFMTF QMSLRREDVW LP LMSYRNS LLAGGDDDTM SVISGISSRG STVRSKKSKP STGKRKVVEG MQLSLTEESS SSDSMWLSRE QTLHTPVMMQ TPQ LTSTIM REPKRLRPED SFMSVYPMQT EHHQTPLDYN RRGTSLMEDD EEPIVEDVMM SSEGRIEDLN EGMDFDTMDI DLPP SKNRR ERTELKPDFF DPASIMDESV LGVSMFSSLA EENLYFQSWS HPQFEKGGGS GGGSGGGSWS HPQFEK UniProtKB: Cohesin subunit SA-2 |
-Macromolecule #2: Double-strand-break repair protein rad21 homolog
| Macromolecule | Name: Double-strand-break repair protein rad21 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 27.693211 KDa |
| Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
| Sequence | String: DITVKETKAK RKRKLIVDSV KELDSKTIRA QLSDYSDIVT TLDLAPPTKK LMMWKETGGV EKLFSLPAQP LWNNRLLKLF TRCLTPLVP EDLRKRRKGG EADNLDEFLK EFENPEVPRE DQQQQHQQRD VIDEPIIEEP SRLQESVMEA SRTNIDESAM P PPPPQGVK ...String: DITVKETKAK RKRKLIVDSV KELDSKTIRA QLSDYSDIVT TLDLAPPTKK LMMWKETGGV EKLFSLPAQP LWNNRLLKLF TRCLTPLVP EDLRKRRKGG EADNLDEFLK EFENPEVPRE DQQQQHQQRD VIDEPIIEEP SRLQESVMEA SRTNIDESAM P PPPPQGVK RKAGQIDPEP VMPPQQVEQM EIPPVELPPE EPPNICQLIP ELELLPEKEK EKEKEKEDDE EEEDEDASGG DQ D UniProtKB: Double-strand-break repair protein rad21 homolog |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.1 mg/mL | ||||||||||||
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| Buffer | pH: 8 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS / Support film - Film thickness: 1 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 277.15 K / Instrument: LEICA EM GP |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Specialist optics | Energy filter - Name: TFS Selectris X / Energy filter - Slit width: 10 eV |
| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 16 / Number real images: 57012 / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 130000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
Switzerland, 2 items
Citation





















Z (Sec.)
Y (Row.)
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Trichoplusia ni (cabbage looper)
Processing
FIELD EMISSION GUN

