|Entry||Database: EMDB / ID: 3851|
|Title||Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM|
|Sample||Beta-amyloid protein 42 fibrils|
|Source||Homo sapiens / human|
|Map data||The density map was sharpened by a B-factor of -50 Ang^2 and filtered to 3.5 Ang. This density map was used for model building and refinement.|
|Method||helical reconstruction, at 4 Å resolution|
|Authors||Gremer L / Schoelzel D|
|Citation||Science, 2017, 358, 116-119|
Science, 2017, 358, 116-119 Yorodumi Papers
|Validation Report||PDB-ID: 5oqv|
SummaryFull reportAbout validation report
|Date||Deposition: Aug 14, 2017 / Header (metadata) release: Sep 13, 2017 / Map release: Sep 13, 2017 / Last update: Oct 18, 2017|
Downloads & links
|File||emd_3851.map.gz (map file in CCP4 format, 40311 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 0.935 Å|
CCP4 map header:
-Entire Beta-amyloid protein 42 fibrils
|Entire||Name: Beta-amyloid protein 42 fibrils / Number of components: 2|
-Component #1: protein, Beta-amyloid protein 42 fibrils
|Protein||Name: Beta-amyloid protein 42 fibrils / Recombinant expression: No|
|Source||Species: Homo sapiens / human|
|Source (engineered)||Expression System: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 /|
-Component #2: protein, Amyloid beta A4 protein
|Protein||Name: Amyloid beta A4 protein / Recombinant expression: No|
|Mass||Theoretical: 4.520087 kDa|
|Source (engineered)||Expression System: Homo sapiens / human|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Delta z: 2.335 Å / Delta phi: -179.275 deg.|
|Sample solution||Buffer solution: in water / pH: 2|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE|
Details: 2.5 microL sample was applied to the grid, blotted for 2.5 s before plunging.
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI ARCTICA|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 24 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 110000 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Image acquisition||Number of digital images: 2026|
-Atomic model buiding
-Oct 4, 2017. Three pioneers of this field were awarded Nobel Prize in Chemistry 2017
Three pioneers of this field were awarded Nobel Prize in Chemistry 2017
- Jacques Dubochet (University of Lausanne, Switzerland) is a pioneer of ice-embedding method of EM specimen (as known as cryo-EM), Most of 3DEM structures in EMDB and PDB are obtained using his method.
- Joachim Frank (Columbia University, New York, USA) is a pioneer of single particle reconstruction, which is the most used reconstruction method for 3DEM structures in EMDB and EM entries in PDB. And also, he is a develper of Spider, which is one of the most famous software in this field, and is used for some EM Navigor data (e.g. map projection/slice images).
- Richard Henderson (MRC Laboratory of Molecular Biology, Cambridge, UK) was determined the first biomolecule structure by EM. The first EM entry in PDB, PDB-1brd is determinedby him.
External links: The 2017 Nobel Prize in Chemistry - Press Release
-Jul 12, 2017. Major update of PDB
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