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Open data
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Basic information
| Entry | ![]() | |||||||||||||||
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| Title | H. sapiens OCCM bound to double stranded DNA | |||||||||||||||
Map data | H. sapiens OCCM bound to double stranded DNA | |||||||||||||||
Sample |
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Keywords | AAA+ ATPase / DNA helicase / REPLICATION | |||||||||||||||
| Function / homology | Function and homology informationDNA replication preinitiation complex assembly / response to sorbitol / positive regulation of chromosome segregation / cellular response to vasopressin / polar body extrusion after meiotic divisions / CDC6 association with the ORC:origin complex / origin recognition complex / positive regulation of DNA-templated DNA replication / regulation of nuclear cell cycle DNA replication / E2F-enabled inhibition of pre-replication complex formation ...DNA replication preinitiation complex assembly / response to sorbitol / positive regulation of chromosome segregation / cellular response to vasopressin / polar body extrusion after meiotic divisions / CDC6 association with the ORC:origin complex / origin recognition complex / positive regulation of DNA-templated DNA replication / regulation of nuclear cell cycle DNA replication / E2F-enabled inhibition of pre-replication complex formation / Switching of origins to a post-replicative state / Unwinding of DNA / negative regulation of DNA-templated DNA replication / nuclear origin of replication recognition complex / traversing start control point of mitotic cell cycle / alpha DNA polymerase:primase complex / Regulation of MITF-M-dependent genes involved in DNA replication, damage repair and senescence / mitotic DNA replication / DNA replication checkpoint signaling / regulation of phosphorylation / CMG complex / attachment of mitotic spindle microtubules to kinetochore / inner kinetochore / nuclear pre-replicative complex / DNA replication preinitiation complex / MCM complex / regulation of cyclin-dependent protein serine/threonine kinase activity / mitotic DNA replication checkpoint signaling / double-strand break repair via break-induced replication / mitotic DNA replication initiation / positive regulation of chromatin binding / Transcription of E2F targets under negative control by DREAM complex / neural precursor cell proliferation / regulation of DNA-templated DNA replication initiation / regulation of mitotic metaphase/anaphase transition / DNA strand elongation involved in DNA replication / negative regulation of DNA replication / positive regulation of cytokinesis / spindle midzone / G1/S-Specific Transcription / negative regulation of cell cycle / regulation of DNA replication / cellular response to angiotensin / DNA replication origin binding / cochlea development / protein polymerization / DNA replication initiation / Activation of the pre-replicative complex / glial cell proliferation / Activation of ATR in response to replication stress / heterochromatin / intercellular bridge / DNA polymerase binding / cellular response to interleukin-4 / DNA helicase activity / protein serine/threonine kinase binding / Assembly of the ORC complex at the origin of replication / cellular response to epidermal growth factor stimulus / positive regulation of DNA replication / Assembly of the pre-replicative complex / helicase activity / kinetochore / CDK-mediated phosphorylation and removal of Cdc6 / cellular response to xenobiotic stimulus / Orc1 removal from chromatin / positive regulation of fibroblast proliferation / spindle pole / mitotic spindle / mitotic cell cycle / nucleosome assembly / single-stranded DNA binding / histone binding / DNA helicase / chromosome, telomeric region / DNA replication / cell population proliferation / nuclear body / cilium / negative regulation of cell population proliferation / cell division / nucleotide binding / intracellular membrane-bounded organelle / apoptotic process / DNA damage response / centrosome / chromatin binding / chromatin / nucleolus / perinuclear region of cytoplasm / enzyme binding / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / zinc ion binding / nucleoplasm / ATP binding / metal ion binding / identical protein binding / nucleus / membrane Similarity search - Function | |||||||||||||||
| Biological species | synthetic construct (others) / Homo sapiens (human) | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||||||||
Authors | Greiwe JF / Weissmann F / Diffley JFX / Costa A | |||||||||||||||
| Funding support | United Kingdom, European Union, 4 items
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Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2019 Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams / ![]() Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks. #1: Journal: Biorxiv / Year: 2024Title: MCM Double Hexamer Loading Visualised with Human Proteins Authors: Weissmann F / Greiwe JF / Puhringer T / Miller TCR / Diffley JFX / Costa A | |||||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_19623.map.gz | 230 MB | EMDB map data format | |
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| Header (meta data) | emd-19623-v30.xml emd-19623.xml | 50.6 KB 50.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_19623_fsc.xml | 13.2 KB | Display | FSC data file |
| Images | emd_19623.png | 144 KB | ||
| Masks | emd_19623_msk_1.map | 244.1 MB | Mask map | |
| Filedesc metadata | emd-19623.cif.gz | 14.2 KB | ||
| Others | emd_19623_half_map_1.map.gz emd_19623_half_map_2.map.gz | 226.2 MB 226.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19623 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19623 | HTTPS FTP |
-Validation report
| Summary document | emd_19623_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
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| Full document | emd_19623_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | emd_19623_validation.xml.gz | 22.2 KB | Display | |
| Data in CIF | emd_19623_validation.cif.gz | 28.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19623 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19623 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8s0eMC ![]() 8s09C ![]() 8s0aC ![]() 8s0bC ![]() 8s0cC ![]() 8s0dC ![]() 8s0fC 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_19623.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | H. sapiens OCCM bound to double stranded DNA | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_19623_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: Half map 1 of the main map
| File | emd_19623_half_map_1.map | ||||||||||||
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| Annotation | Half map 1 of the main map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map 2 of the main map
| File | emd_19623_half_map_2.map | ||||||||||||
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| Annotation | Half map 2 of the main map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
+Entire : H. sapiens OCCM bound to double stranded DNA
+Supramolecule #1: H. sapiens OCCM bound to double stranded DNA
+Supramolecule #2: Double stranded DNA
+Supramolecule #3: H. sapiens OCCM
+Macromolecule #1: DNA (39-mer)
+Macromolecule #2: DNA (39-mer)
+Macromolecule #3: DNA replication licensing factor MCM5
+Macromolecule #4: DNA replication factor Cdt1
+Macromolecule #5: DNA replication licensing factor MCM2
+Macromolecule #6: DNA replication licensing factor MCM4
+Macromolecule #7: DNA replication licensing factor MCM6
+Macromolecule #8: DNA replication licensing factor MCM7
+Macromolecule #9: Origin recognition complex subunit 2
+Macromolecule #10: Origin recognition complex subunit 3
+Macromolecule #11: Cell division control protein 6 homolog
+Macromolecule #12: DNA replication licensing factor MCM3
+Macromolecule #13: Origin recognition complex subunit 1
+Macromolecule #14: Origin recognition complex subunit 4
+Macromolecule #15: Origin recognition complex subunit 5
+Macromolecule #16: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
+Macromolecule #17: MAGNESIUM ION
+Macromolecule #18: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GRAPHENE OXIDE |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV |
| Details | The MCM recruitment reaction was reconstituted in vitro using purified H. sapiens proteins, a short DNA template and ATPgammaS. Four microlitres of the entire reaction was applied on a grid and incubated for 1 min at room temperature before blotting with filter paper for 5 s and plunge-freezing in liquid ethane. |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum |
| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 31569 / Average exposure time: 9.4 sec. / Average electron dose: 49.28 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 130000 |
| Sample stage | 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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| Output model | ![]() PDB-8s0e: |
Movie
Controller
About Yorodumi




Keywords
Homo sapiens (human)
Authors
United Kingdom, European Union, 4 items
Citation






















Z (Sec.)
Y (Row.)
X (Col.)














































FIELD EMISSION GUN




