|Entry||Database: PDB / ID: 5oh0|
|Title||The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod|
|Descriptor||Type-1 fimbrial protein, A chain|
|Keywords||PROTEIN FIBRIL / bacterial pilus / chaperone-usher pilus|
|Specimen source||Escherichia coli j96 / bacteria / image: Escherichia coli|
|Method||Electron microscopy (4.2 Å resolution / Helical array / Helical)|
|Authors||Hospenthal, M.K. / Costa, T.R.D. / Redzej, A. / Waksman, G.|
|Citation||Structure, 2017, 25, 1829-1838.e4|
SummaryFull reportAbout validation report
|Date||Deposition: Jul 13, 2017 / Release: Nov 22, 2017|
Downloads & links
A: Type-1 fimbrial protein, A chain
B: Type-1 fimbrial protein, A chain
C: Type-1 fimbrial protein, A chain
D: Type-1 fimbrial protein, A chain
E: Type-1 fimbrial protein, A chain
F: Type-1 fimbrial protein, A chain
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: HELICAL ARRAY / Reconstruction method: HELICAL|
|Component||Name: Type 1 Chaperone-usher pilus / Type: COMPLEX|
Details: Superhelical assembly of the pilus rod subunit FimA
Entity ID: 1 / Source: RECOMBINANT
|Molecular weight||Experimental value: NO|
|Source (natural)||Organism: Escherichia coli J96|
|Source (recombinant)||Organism: Escherichia coli HB101|
|Buffer solution||pH: 7.5|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid type: Quantifoil 1.2/1.3 400 mesh grid|
|Vitrification||Cryogen name: ETHANE / Humidity: 95 %|
-Electron microscopy imaging
Model: Tecnai Polara / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI POLARA 300|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELD|
|Image recording||Electron dose: 1.7 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|Software||Name: PHENIX / Version: dev_2776: / Classification: refinement|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Helical symmerty||Angular rotation/subunit: 114.992 deg. / Axial rise/subunit: 8.01188 Å / Axial symmetry: C1|
|Particle selection||Number of particles selected: 115545|
|3D reconstruction||Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 115510 / Symmetry type: HELICAL|
|Atomic model building|
|Refine LS restraints|
-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
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