+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-18307 | |||||||||||||||
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Title | Native eisosome lattice bound to plasma membrane microdomain | |||||||||||||||
Map data | Native eisosome lattice - sharpened map | |||||||||||||||
Sample |
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Keywords | BAR domain / plasma membrane microdomain / membrane curvature / native biochemistry / LIPID BINDING PROTEIN | |||||||||||||||
Function / homology | Function and homology information protein localization to eisosome filament / eisosome filament / eisosome assembly / eisosome / lipid droplet / cell periphery / endocytosis / protein localization / response to heat / mitochondrial outer membrane ...protein localization to eisosome filament / eisosome filament / eisosome assembly / eisosome / lipid droplet / cell periphery / endocytosis / protein localization / response to heat / mitochondrial outer membrane / lipid binding / mitochondrion / plasma membrane / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||||||||
Authors | Kefauver JM / Zou L / Loewith RJ / Defosses A | |||||||||||||||
Funding support | European Union, Switzerland, 4 items
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Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2018 Title: Real-space refinement in PHENIX for cryo-EM and crystallography. Authors: Pavel V Afonine / Billy K Poon / Randy J Read / Oleg V Sobolev / Thomas C Terwilliger / Alexandre Urzhumtsev / Paul D Adams / Abstract: This article describes the implementation of real-space refinement in the phenix.real_space_refine program from the PHENIX suite. The use of a simplified refinement target function enables very fast ...This article describes the implementation of real-space refinement in the phenix.real_space_refine program from the PHENIX suite. The use of a simplified refinement target function enables very fast calculation, which in turn makes it possible to identify optimal data-restraint weights as part of routine refinements with little runtime cost. Refinement of atomic models against low-resolution data benefits from the inclusion of as much additional information as is available. In addition to standard restraints on covalent geometry, phenix.real_space_refine makes use of extra information such as secondary-structure and rotamer-specific restraints, as well as restraints or constraints on internal molecular symmetry. The re-refinement of 385 cryo-EM-derived models available in the Protein Data Bank at resolutions of 6 Å or better shows significant improvement of the models and of the fit of these models to the target maps. | |||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_18307.map.gz | 59.7 MB | EMDB map data format | |
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Header (meta data) | emd-18307-v30.xml emd-18307.xml | 41 KB 41 KB | Display Display | EMDB header |
Images | emd_18307.png | 134.8 KB | ||
Filedesc metadata | emd-18307.cif.gz | 6.7 KB | ||
Others | emd_18307_additional_1.map.gz emd_18307_additional_10.map.gz emd_18307_additional_11.map.gz emd_18307_additional_2.map.gz emd_18307_additional_3.map.gz emd_18307_additional_4.map.gz emd_18307_additional_5.map.gz emd_18307_additional_6.map.gz emd_18307_additional_7.map.gz emd_18307_additional_8.map.gz emd_18307_additional_9.map.gz emd_18307_half_map_1.map.gz emd_18307_half_map_2.map.gz | 31.8 MB 271.1 MB 59.8 MB 267.4 MB 272.9 MB 273.9 MB 274.1 MB 272.7 MB 271.2 MB 272 MB 266.6 MB 59.3 MB 59.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18307 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18307 | HTTPS FTP |
-Validation report
Summary document | emd_18307_validation.pdf.gz | 865 KB | Display | EMDB validaton report |
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Full document | emd_18307_full_validation.pdf.gz | 864.6 KB | Display | |
Data in XML | emd_18307_validation.xml.gz | 12.2 KB | Display | |
Data in CIF | emd_18307_validation.cif.gz | 14.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18307 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18307 | HTTPS FTP |
-Related structure data
Related structure data | 8qb7MC 8qb8MC 8qb9C 8qbbC 8qbdC 8qbeC 8qbfC 8qbgC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_18307.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Native eisosome lattice - sharpened map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.327 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
+Additional map: Native eisosome lattice - unsharpened map
+Additional map: Native eisosome helical map (C2, rise=11.00, twist=54.02)
+Additional map: Native eisosome lattice - deepEMhancer sharpened map
+Additional map: Native eisosome helical map (C4, rise=21.27, twist=50.99)
+Additional map: Native eisosome helical map (C7, rise=37.28, twist=36.72)
+Additional map: Native eisosome helical map (C1, rise=5.58, twist=53.51)
+Additional map: Native eisosome helical map (C1, rise=5.13, twist=49.32)
+Additional map: Native eisosome helical map (C1, rise=5.2, twist=136.56)
+Additional map: Native eisosome helical map (C2, rise=10.02, twist=47.98)
+Additional map: Native eisosome helical map (C1, rise=4.89, twist=46.59)
+Additional map: Native eisosome helical map (C8, rise=37.41, twist=57.83)
+Half map: Native eisosome lattice - half map B
+Half map: Native eisosome lattice - half map A
-Sample components
-Entire : Helical lattice of native Pil1/Lsp1 protein bound to plasma membr...
Entire | Name: Helical lattice of native Pil1/Lsp1 protein bound to plasma membrane microdomain |
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Components |
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-Supramolecule #1: Helical lattice of native Pil1/Lsp1 protein bound to plasma membr...
Supramolecule | Name: Helical lattice of native Pil1/Lsp1 protein bound to plasma membrane microdomain type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: TB50 / Organelle: eisosome / Location in cell: plasma membrane |
-Macromolecule #1: Sphingolipid long chain base-responsive protein PIL1
Macromolecule | Name: Sphingolipid long chain base-responsive protein PIL1 / type: protein_or_peptide / ID: 1 / Number of copies: 14 / Enantiomer: LEVO |
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Source (natural) | Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: TB50 |
Molecular weight | Theoretical: 38.393043 KDa |
Sequence | String: MHRTYSLRNS RAPTASQLQN PPPPPSTTKG RFFGKGGLAY SFRRSAAGAF GPELSRKLSQ LVKIEKNVLR SMELTANERR DAAKQLSIW GLENDDDVSD ITDKLGVLIY EVSELDDQFI DRYDQYRLTL KSIRDIEGSV QPSRDRKDKI TDKIAYLKYK D PQSPKIEV ...String: MHRTYSLRNS RAPTASQLQN PPPPPSTTKG RFFGKGGLAY SFRRSAAGAF GPELSRKLSQ LVKIEKNVLR SMELTANERR DAAKQLSIW GLENDDDVSD ITDKLGVLIY EVSELDDQFI DRYDQYRLTL KSIRDIEGSV QPSRDRKDKI TDKIAYLKYK D PQSPKIEV LEQELVRAEA ESLVAEAQLS NITRSKLRAA FNYQFDSIIE HSEKIALIAG YGKALLELLD DSPVTPGETR PA YDGYEAS KQIIIDAESA LNEWTLDSAQ VKPTLSFKQD YEDFEPEEGE EEEEEDGQGR WSEDEQEDGQ IEEPEQEEEG AVE EHEQVG HQQSESLPQQ TTA UniProtKB: Sphingolipid long chain base-responsive protein PIL1 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | helical array |
-Sample preparation
Buffer | pH: 7 / Details: 50mM PIPES pH 7, 300mM NaCl, 1mM CHAPS, 0.5mM DTT |
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Grid | Model: EMS Lacey Carbon / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: LACEY |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER / Details: Cylindrical map |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.1.2) / Number images used: 2423944 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0.8) |
Final angle assignment | Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.1.2) |