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Open data
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Basic information
Entry | ![]() | ||||||||||||||||||
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Title | mouse Seipin complex | ||||||||||||||||||
![]() | mouse seipin complex | ||||||||||||||||||
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![]() | seipin / lipid droplets / adipose / MEMBRANE PROTEIN | ||||||||||||||||||
Function / homology | Seipin family / Putative adipose-regulatory protein (Seipin) / lipid droplet formation / lipid droplet / phospholipid binding / lipid metabolic process / endoplasmic reticulum membrane / Seipin![]() | ||||||||||||||||||
Biological species | ![]() ![]() | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.19 Å | ||||||||||||||||||
![]() | Li C / Han Y / Wynn RM / Chen Z / Scherer PE | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Adipogenin Dictates Adipose Tissue Expansion by Facilitating the Assembly of a Dodecameric Seipin Complex Authors: Li C / Sun X | ||||||||||||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 189.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.7 KB 17.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.7 KB | Display | ![]() |
Images | ![]() | 70.4 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 200.6 MB 200.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 835.1 KB | Display | ![]() |
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Full document | ![]() | 834.6 KB | Display | |
Data in XML | ![]() | 21.6 KB | Display | |
Data in CIF | ![]() | 28.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9c8eMC ![]() 9c8dC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | mouse seipin complex | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.8344 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Seipin complex
Entire | Name: Seipin complex |
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Components |
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-Supramolecule #1: Seipin complex
Supramolecule | Name: Seipin complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 700 KDa |
-Macromolecule #1: Seipin
Macromolecule | Name: Seipin / type: protein_or_peptide / ID: 1 / Number of copies: 11 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 50.993406 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MSGRWSHPQF EKIHQRREAG ARETCRDQIK GSDKDEEPSA ALSHGQGYRP CGRPARNSKP EAGARPPAVP IMVNDPPVPA LLWAQEVGH VLAGRARRLM LQFGVLFCTI LLLLWVSVFL YGSFYYSYMP TVSHLSPVHF HYRTDCDSST ASLCSFPVAN V SLAKSGRD ...String: MSGRWSHPQF EKIHQRREAG ARETCRDQIK GSDKDEEPSA ALSHGQGYRP CGRPARNSKP EAGARPPAVP IMVNDPPVPA LLWAQEVGH VLAGRARRLM LQFGVLFCTI LLLLWVSVFL YGSFYYSYMP TVSHLSPVHF HYRTDCDSST ASLCSFPVAN V SLAKSGRD RVLMYGQPYR VTLELELPES PVNQDLGMFL VTVSCYTRGG RIISTSSRSV MLHYRSQLLQ VLDTLLFSSL LL FGFAEQK QLLEVELYSD YRENSYVPTT GAIIEIHSKR IQMYGAYLRI HAHFTGLRYL LYNFPMTCAF VGVASNFTFL SVI VLFSYM QWVWGAVWPR HRFSLQVNIR QRDNSHHGAP RRISRHQPGQ ESTQQSDVTE DGESPEDPSG TEGQLSEEEK PEKR PLNGE EEQEPEASDG SWEDAALLTE ANPPTSASAS ALAPETLGSL RQRPTCSSS UniProtKB: Seipin |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |