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Open data
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Basic information
| Entry | ![]() | ||||||||||||
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| Title | NONO/SFPQ filament: local refinement central units (strand 1) | ||||||||||||
Map data | local refinement, sharpened with Phenix-autosharpen B = 50 | ||||||||||||
Sample |
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Keywords | filament / RNA binding / DNA binding / gene regulation / NUCLEAR PROTEIN | ||||||||||||
| Function / homology | Function and homology informationdendritic transport of messenger ribonucleoprotein complex / positive regulation of sister chromatid cohesion / negative regulation of circadian rhythm / alternative mRNA splicing, via spliceosome / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / paraspeckles / chromosome organization / activation of innate immune response / double-strand break repair via homologous recombination ...dendritic transport of messenger ribonucleoprotein complex / positive regulation of sister chromatid cohesion / negative regulation of circadian rhythm / alternative mRNA splicing, via spliceosome / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / paraspeckles / chromosome organization / activation of innate immune response / double-strand break repair via homologous recombination / regulation of circadian rhythm / RNA polymerase II transcription regulator complex / histone deacetylase binding / nuclear matrix / fibrillar center / transcription cis-regulatory region binding / nuclear speck / chromatin remodeling / innate immune response / negative regulation of DNA-templated transcription / dendrite / chromatin binding / chromatin / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / RNA binding / identical protein binding Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||
Authors | Rasmussen T / Bottcher B | ||||||||||||
| Funding support | Germany, 3 items
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Citation | Journal: to be publishedTitle: A filamentous scaffold for gene regulation Authors: Rasmussen T / Kuspert J / Schonemann L / Geiger D / Bottcher B | ||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_51438.map.gz | 407.4 MB | EMDB map data format | |
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| Header (meta data) | emd-51438-v30.xml emd-51438.xml | 25.4 KB 25.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51438_fsc.xml | 17 KB | Display | FSC data file |
| Images | emd_51438.png | 106.8 KB | ||
| Masks | emd_51438_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-51438.cif.gz | 6.9 KB | ||
| Others | emd_51438_half_map_1.map.gz emd_51438_half_map_2.map.gz | 475.3 MB 475.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51438 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51438 | HTTPS FTP |
-Validation report
| Summary document | emd_51438_validation.pdf.gz | 788.9 KB | Display | EMDB validaton report |
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| Full document | emd_51438_full_validation.pdf.gz | 788.4 KB | Display | |
| Data in XML | emd_51438_validation.xml.gz | 26.4 KB | Display | |
| Data in CIF | emd_51438_validation.cif.gz | 35 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51438 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51438 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9glcMC ![]() 9gldC ![]() 9gniC 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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Map
| File | Download / File: emd_51438.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | local refinement, sharpened with Phenix-autosharpen B = 50 | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.946 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_51438_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: half map A
| File | emd_51438_half_map_1.map | ||||||||||||
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| Annotation | half map A | ||||||||||||
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| Density Histograms |
-Half map: half map B
| File | emd_51438_half_map_2.map | ||||||||||||
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| Annotation | half map B | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : NONO/SFPQ filament
| Entire | Name: NONO/SFPQ filament |
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| Components |
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-Supramolecule #1: NONO/SFPQ filament
| Supramolecule | Name: NONO/SFPQ filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: filaments formed by concentrating to 1 mg/ml |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Splicing factor proline/glutamine rich (polypyrimidine tract bind...
| Macromolecule | Name: Splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated) type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 75.880156 KDa |
| Sequence | String: MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGGPKPPIPP PPPHQQQPQQ PPPQQPPPQQ PPPHQQPPP HQPPHQQPPP PPQDSSKPVV PQGPGSAPGV SPAPPPAGSA PPANPPTTGA PPGPGPTPTP PPAVTSATPG P PPPSTPSS ...String: MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGGPKPPIPP PPPHQQQPQQ PPPQQPPPQQ PPPHQQPPP HQPPHQQPPP PPQDSSKPVV PQGPGSAPGV SPAPPPAGSA PPANPPTTGA PPGPGPTPTP PPAVTSATPG P PPPSTPSS GVSTTPPQSG GPPPPPAGGA GPGPKQGPGP GPGGPKGGKM PGGPKPGGGP GMGAPGGHPK PPHRGGGEPR GG RQHHPPY HQQHHQGPPP GGPAARTEEK ISDSEGFKAN LSLLRRPGEK TYTQRCRLFV GNLPADITED EFKRLFAKYG EPG EVFINK GKGFGFIKLE SRALAEIAKA ELDDTPMRGR QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA VVIV DDRGR STGKGIVEFA SKPAARKAFE RCSEGVFLLT TTPRPVIVEP LEQLDDEDGL PEKLAQKNPM YQKERETPPR FAQHG TFEY EYSQRWKSLD EMEKQQREQV EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR MEELHSQEMQ KRKEMQ LRQ EEERRRREEE MMIRQREMEE QMRRQREESY SRMGYMDPRE RDMRMGGGGT MNMGDPYGSG GQKFPPLGGG GGIGYEA NP GVPPATMSGS MMGSDMRTER FGQGGAGPVG GQGPRGMGPG TPAGYGRGRE EYEGPNKKPR F UniProtKB: Splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated) |
-Macromolecule #2: Non-POU domain containing octamer binding
| Macromolecule | Name: Non-POU domain containing octamer binding / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 54.519828 KDa |
| Sequence | String: MQSNKTFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQPPP PIPANGQQAS SQNEGLTIDL KNFRKPGEKT FTQRSRLFVG NLPPDITEE EMRKLFEKYG KAGEVFIHKD KGFGFIRLET RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA SLTVRNLPQY V SNELLEEA ...String: MQSNKTFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQPPP PIPANGQQAS SQNEGLTIDL KNFRKPGEKT FTQRSRLFVG NLPPDITEE EMRKLFEKYG KAGEVFIHKD KGFGFIRLET RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA SLTVRNLPQY V SNELLEEA FSVFGQVERA VVIVDDRGRP SGKGIVEFSG KPAARKALDR CSEGSFLLTT FPRPVTVEPM DQLDDEEGLP EK LVIKNQQ FHKEREQPPR FAQPGSFEYE YAMRWKALIE MEKQQQDQVD RNIKEAREKL EMEMEAARHE HQVMLMRQDL MRR QEELRR MEELHNQEVQ KRKQLELRQE EERRRREEEM RRQQEEMMRR QQEGFKGTFP DAREQEIRMG QMAMGGAMGI NNRG AMPPA PVPTGTPAPP GPATMMPDGT LGLTPPTTER FGQAATMEGI GAIGGTPPAF NRPAPGADFA PNKRRRY UniProtKB: Non-POU domain-containing octamer-binding protein |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | filament |
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Sample preparation
| Concentration | 1 mg/mL | ||||||||||||||||||
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| Buffer | pH: 7.5 Component:
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| Grid | Model: Quantifoil R0.6/1 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 150 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.04 kPa | ||||||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blot time 5 sec, blot force +20. |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: TFS Selectris / Energy filter - Slit width: 5 eV |
| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 17059 / Average exposure time: 6.2 sec. / Average electron dose: 70.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.4000000000000001 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 130000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model |
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| Details | first rigid fitting with Chimera, then further refinemnt with Coot, C-terminal some de-novo residues | |||||||||
| Refinement | Space: REAL / Protocol: FLEXIBLE FIT | |||||||||
| Output model | ![]() PDB-9glc: |
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About Yorodumi




Keywords
Authors
Germany, 3 items
Citation







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Y (Row.)
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FIELD EMISSION GUN


