EMD-6429

Single-particle
30.0 Å
EMD-6429 Deposition: 17/08/2015
Map released: 09/09/2015
Last modified: 14/10/2015
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EMD-6429

Architecture of the complex formed by large and small Terminase subunits from Bacteriophage P22

EMD-6429

Single-particle
30.0 Å
EMD-6429 Deposition: 17/08/2015
Map released: 09/09/2015
Last modified: 14/10/2015
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Method: Single-particle
Aggregation State: Particle
Specimen preparation [1]
Concentration: 0.014 mg/mL
Buffer
pH: 8.0
Details: 20 mM Tris-HCl, 150 mM NaCl, 3 mm DTT, 5% glycerol, 1 mM MgCl2
Staining
Type: NEGATIVE
Details: Protein was adsorbed to the grid for 1 minute, blotted, and passed through four consecutive 40 microliter drops of 2% uranyl formate.
Grid
Details: 400 mesh copper grids charged with Gatan plasma cleaner
Vitrification
Cryogen name: NONE
Instrument: OTHER
Microscopy [1]
Microscope: FEI TECNAI 12
Illumination mode: FLOOD BEAM
Imaging mode: BRIGHT FIELD
Electron source: FIELD EMISSION GUN
Acceleration voltage: 120 kV
Nominal defocus: 0.1 µm - 0.2 µm
Nominal magnification: 52000.0
Specimen holder model: SIDE ENTRY, EUCENTRIC
Image Recording [1]
Detector category: CCD
Detector model: TVIPS TEMCAM-F416 (4k x 4k)
Number of real images: 44
Average electron dose per image: 20 e/Å2
Details: Images were acquired using Leginon.
Image processing [1]
Details: Particles were selected and filtered using the Appion Suite. Refinement was done with RELION.
Final reconstruction
Resolution: 30.0 Å ( BY AUTHOR)
Resolution method: OTHER
Number of images used: 2062
Algorithm: OTHER
Details:
Software [1]
Name Version Details
RELION - -
Map
Format: CCP4
Data type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation details: Asymmetric reconstruction of terminase holoenzyme from Bacteriophage P22
Details: ::::EMDATABANK.org::::EMD-6429::::
Geometry
X Y Z
Dimensions 72 72 72
Origin 0 0 0
Spacing 72 72 72
Voxel size 4.1 Å 4.1 Å 4.1 Å
Contour list
Primary Level Source
True 0.022 AUTHOR