|Entry||Database: EMDB / ID: 1134|
|Title||Polymorphism and double hexamer structure in the archaeal minichromosome maintenance (MCM) helicase from Methanobacterium thermoautotrophicum.|
|Sample||Archaeal helicase MCM from Methanobacterium thermoautotrophicum|
|Source||Methanothermobacter thermautotrophicus / archaea / thermophilic / Methanobacterium thermoautotrophicum / メタノサーモバクター・サームオートトロフィカス|
|Map data||test map|
|Method||single particle reconstruction, at 25 Å resolution|
|Authors||Gomez-Llorente Y / Fletcher RJ / Chen XS / Carazo JM / San Martin C|
|Citation||J. Biol. Chem., 2005, 280, 40909-40915|
|Date||Deposition: Mar 16, 2005 / Header (metadata) release: Jul 1, 2005 / Map release: Jul 1, 2006 / Last update: May 26, 2011|
Downloads & links
|File||emd_1134.map.gz (map file in CCP4 format, 3457 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 3.5 Å|
CCP4 map header:
-Entire Archaeal helicase MCM from Methanobacterium thermoautotrophicum
|Entire||Name: Archaeal helicase MCM from Methanobacterium thermoautotrophicum|
Oligomeric State: homododecamer / Number of components: 1
|Mass||Theoretical: 900 kDa / Experimental: 900 kDa / Measured by: gel filtration|
-Component #1: protein, minichromosome maintenance protein
|Protein||Name: minichromosome maintenance protein / a.k.a: MCM / Oligomeric Details: dodecamer / Recombinant expression: Yes / Number of Copies: 12|
|Mass||Theoretical: 75.6 MDa / Experimental: 75.6 MDa|
|Source||Species: Methanothermobacter thermautotrophicus / archaea / thermophilic / Methanobacterium thermoautotrophicum / メタノサーモバクター・サームオートトロフィカス|
Strain: Delta H
|Source (engineered)||Expression System: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 /|
|External references||InterPro: InterPro: 001208 / Gene Ontology: GO: 0006270|
|Sample solution||Specimen conc.: 0.1 mg/ml|
Buffer solution: 50 mM Tris.HCl pH 8.0, 1 mM DTT, 50 mM to 1M NaCl
|Support film||glow discharged, collodion/carbon coated copper grids|
|Staining||2% uranyl acetate|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
|Imaging||Microscope: JEOL 1200EXII|
Details: he make and model of the microscope. Jeol 1200 EX-II. Standard Jeol 1200 holder
|Electron gun||Electron source: TUNGSTEN HAIRPIN / Accelerating voltage: 80 kV / Electron dose: 10 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 60000 X (nominal) / Astigmatism: visually corrected at 100,000x / Cs: 5.6 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Holder: side entry / Model: OTHER|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Scanner: ZEISS SCAI / Sampling size: 7 microns / Bit depth: 8|
|Processing||Method: single particle reconstruction / Number of projections: 1200 / Applied symmetry: C6 (6 fold cyclic)|
|3D reconstruction||Algorithm: projection matching / Software: SPIDER, XMIPP / Resolution: 25 Å / Resolution method: 3D SSNR = 1|
Euler angles: theta between 75 and 90, phi between 0 and 360
Details: reconstructed with ART
-Atomic model buiding
|Modeling #1||Software: Amira|
-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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