+
Open data
-
Basic information
| Entry | ![]() | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | Cryo-EM structure of the human SAM50-engaged SAM complex | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | SAM complex / SAM50-engaged. / TRANSLOCASE | |||||||||
| Function / homology | Function and homology informationMIB complex / mitochondrial outer membrane translocase complex assembly / SAM complex / Cristae formation / inner mitochondrial membrane organization / cristae formation / protein insertion into mitochondrial outer membrane / Mitochondrial protein import / mitochondrial transport / protein import into mitochondrial matrix ...MIB complex / mitochondrial outer membrane translocase complex assembly / SAM complex / Cristae formation / inner mitochondrial membrane organization / cristae formation / protein insertion into mitochondrial outer membrane / Mitochondrial protein import / mitochondrial transport / protein import into mitochondrial matrix / RAC2 GTPase cycle / mitochondrial outer membrane / mitochondrion / extracellular exosome / membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Yan L / Guan Z / Wang Q / Yin P | |||||||||
| Funding support | China, 1 items
| |||||||||
Citation | Journal: To Be PublishedTitle: Mechanical Insights into the SAM-mediated Mitochondrial beta-barrel outer membrane protein folding in Mammalian Cells Authors: Guan Z / Yan L / Yin P | |||||||||
| History |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_80423.map.gz | 75.2 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-80423-v30.xml emd-80423.xml | 15.1 KB 15.1 KB | Display Display | EMDB header |
| Images | emd_80423.png | 85.9 KB | ||
| Filedesc metadata | emd-80423.cif.gz | 5.6 KB | ||
| Others | emd_80423_half_map_1.map.gz emd_80423_half_map_2.map.gz | 77.7 MB 77.7 MB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-80423 ftp://data.pdbj.org/pub/emdb/structures/EMD-80423 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 25wfMC ![]() 25wgC M: atomic model generated by this map C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|---|
| Related items in Molecule of the Month |
-
Map
| File | Download / File: emd_80423.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-Half map: #1
| File | emd_80423_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #2
| File | emd_80423_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-
Sample components
-Entire : SAM50-engaged SAM complex
| Entire | Name: SAM50-engaged SAM complex |
|---|---|
| Components |
|
-Supramolecule #1: SAM50-engaged SAM complex
| Supramolecule | Name: SAM50-engaged SAM complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Sorting and assembly machinery component 50 homolog
| Macromolecule | Name: Sorting and assembly machinery component 50 homolog / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 54.364301 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MDYKDDDDKG DYKDDDDKGS MGTVHARSLE PLPSSGPDFG GLGEEAEFVE VEPEAKQEIL ENKDVVVQHV HFDGLGRTKD DIIICEIGD VFKAKNLIEV MRKSHEAREK LLRLGIFRQV DVLIDTCQGD DALPNGLDVT FEVTELRRLT GSYNTMVGNN E GSMVLGLK ...String: MDYKDDDDKG DYKDDDDKGS MGTVHARSLE PLPSSGPDFG GLGEEAEFVE VEPEAKQEIL ENKDVVVQHV HFDGLGRTKD DIIICEIGD VFKAKNLIEV MRKSHEAREK LLRLGIFRQV DVLIDTCQGD DALPNGLDVT FEVTELRRLT GSYNTMVGNN E GSMVLGLK LPNLLGRAEK VTFQFSYGTK ETSYGLSFFK PRPGNFERNF SVNLYKVTGQ FPWSSLRETD RGMSAEYSFP IW KTSHTVK WEGVWRELGC LSRTASFAVR KESGHSLKSS LSHAMVIDSR NSSILPRRGA LLKVNQELAG YTGGDVSFIK EDF ELQLNK QLIFDSVFSA SFWGGMLVPI GDKPSSIADR FYLGGPTSIR GFSMHSIGPQ SEGDYLGGEA YWAGGLHLYT PLPF RPGQG GFGELFRTHF FLNAGNLCNL NYGEGPKAHI RKLAECIRWS YGAGIVLRLG NIARLELNYC VPMGVQTGDR ICDGV QFGA GIRFL UniProtKB: Sorting and assembly machinery component 50 homolog |
-Macromolecule #2: Metaxin-2
| Macromolecule | Name: Metaxin-2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 33.06757 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MSLVAEAFVS QIAAAEPWPE NATLYQQLKG EQILLSDNAA SLAVQAFLQM CNLPIKVVCR ANAEYMSPSG KVPFIHVGNQ VVSELGPIV QFVKAKGHSL SDGLEEVQKA EMKAYMELVN NMLLTAELYL QWCDEATVGE ITHARYGSPY PWPLNHILAY Q KQWEVKRK ...String: MSLVAEAFVS QIAAAEPWPE NATLYQQLKG EQILLSDNAA SLAVQAFLQM CNLPIKVVCR ANAEYMSPSG KVPFIHVGNQ VVSELGPIV QFVKAKGHSL SDGLEEVQKA EMKAYMELVN NMLLTAELYL QWCDEATVGE ITHARYGSPY PWPLNHILAY Q KQWEVKRK MKAIGWGKKT LDQVLEDVDQ CCQALSQRLG TQPYFFNKQP TELDALVFGH LYTILTTQLT NDELSEKVKN YS NLLAFCR RIEQHYFEDR GKGRLSLESA WSHPQFEKGG GSGGGSGGSA WSHPQFEK UniProtKB: Metaxin-2 |
-Experimental details
-Structure determination
| Method | cryo EM |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | particle |
-
Sample preparation
| Concentration | 5 mg/mL |
|---|---|
| Buffer | pH: 7.4 |
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 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: 2.2 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
Movie
Controller
About Yorodumi




Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation





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




































Processing
FIELD EMISSION GUN
