|Entry||Database: EMDB / ID: 5936|
|Title||Electron cryo-microscopy of the Moloney murine leukemia virus furin precursor Env in its native form|
|Map data||Reconstruction of the native furin cleavage deficient mutant (R466G/K468G) Env of Moloney murine leukemia virus|
|Sample||Native form of furin cleavage deficient mutant (R466G/K468G) Env of Moloney murine leukemia virus:|
|Keywords||Furin precursor / Moloney murine leukemia virus / Env maturation|
|Source||Moloney murine leukemia virus|
|Method||single particle reconstruction / cryo EM / 22 Å resolution|
|Authors||Sjoberg M / Wu SR / Loving R / Rantalainen K / Lindqvist B / Garoff H|
|Citation||Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2014|
Title: Furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure.
Authors: Mathilda Sjöberg / Shang-Rung Wu / Robin Löving / Kimmo Rantalainen / Birgitta Lindqvist / Henrik Garoff
|Date||Deposition: Mar 28, 2014 / Header (metadata) release: Apr 9, 2014 / Map release: Apr 9, 2014 / Last update: May 14, 2014|
|Structure viewer||EM map: |
Downloads & links
|File||emd_5936.map.gz (map file in CCP4 format, 433 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 3.5 Å|
CCP4 map header:
-Entire Native form of furin cleavage deficient mutant (R466G/K468G) Env ...
|Entire||Name: Native form of furin cleavage deficient mutant (R466G/K468G) Env of Moloney murine leukemia virus|
Details: Affinity purified, gradient separated protein in 0.05% Triton X-100
Number of components: 1 / Oligomeric State: trimer
|Mass||Theoretical: 270 kDa / Experimental: 500 kDa / Measured by: Estimated from Blue native PAGE|
-Component #1: protein, gp90
|Protein||Name: gp90 / a.k.a: Furin precursor / Oligomeric Details: Trimer / Recombinant expression: No / Number of Copies: 3|
|Mass||Theoretical: 270 kDa / Experimental: 500 kDa|
|Source||Species: Moloney murine leukemia virus|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.1 mg/ml|
Buffer solution: 50 mM HEPES, 100 mM NaCl, 1.8 mM CaCl2, pH 7.4
|Support film||400 mesh holey carbon grid, glow discharged|
|Vitrification||Instrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Temperature: 77 K / Humidity: 90 %|
Method: Blotted for 3 seconds before plunging in liquid ethane, followed by transfer into liquid nitrogen.
-Electron microscopy imaging
|Imaging||Microscope: JEOL 2100F / Date: Jan 25, 2013|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 9 e/Å2 / Illumination mode: SPOT SCAN|
|Lens||Magnification: 43200 X (nominal), 43200 X (calibrated)|
Astigmatism: Objective lens astigmatism was corrected using online FFT.
Cs: 2 mm / Imaging mode: BRIGHT FIELD / Defocus: 2500 - 4000 nm
|Specimen Holder||Model: GATAN LIQUID NITROGEN / Temperature: 95 K ( 93 - 96 K)|
|Camera||Detector: TVIPS TEMCAM-F416 (4k x 4k)|
|Image acquisition||Number of digital images: 1213 / Sampling size: 3.5 microns / Bit depth: 14|
|Processing||Method: single particle reconstruction / Number of class averages: 30 / Applied symmetry: C3 (3 fold cyclic) / Number of projections: 9802|
Details: The particles were selected using a semi-automatic selection program in EMAN.
|3D reconstruction||Algorithm: back projection / Euler angles: EMAN / Software: EMAN1, EMAN2 / CTF correction: Each particle|
Details: Final maps were calculated from seven averaged datasets. The particles were selected using an automatic selection program. Damaged particles were removed after visual inspection.
Resolution: 22 Å / Resolution method: FSC 0.5, semi-independent
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