EMD-2539

Single-particle
20.0 Å
EMD-2539
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Deposition: 30/12/2013
Map released: 05/02/2014
Last modified: 12/02/2014
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EMD-2539
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cryo-electron microscopy of microtubule-bound human kinesin-5 motor domain in the ADP state (gold cluster in the neck linker V365C).

EMD-2539

Single-particle
20.0 Å
EMD-2539
3D View Gallery
Deposition: 30/12/2013
Map released: 05/02/2014
Last modified: 12/02/2014
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Method: Single-particle
Aggregation State: Particle
Specimen preparation [1]
Buffer
pH: 6.8
Details: 20 mM PIPES, 5 mM MgCl2, 1 mM EGTA, 10 mM ADP, 2% glycerol
Grid
Details: 400 mesh holey carbon grids
Vitrification
Cryogen name: ETHANE
Chamber humidity: 100%
Instrument: FEI VITROBOT MARK I
Method: chamber at 24 degrees C, blot 3.5 sec
Microscopy [1]
Microscope: FEI TECNAI F20
Illumination mode: FLOOD BEAM
Imaging mode: BRIGHT FIELD
Electron source: FIELD EMISSION GUN
Acceleration voltage: 200 kV
Nominal CS: 2.0 mm
Nominal defocus: 1.1 µm - 2.6 µm
Calibrated magnification: 68000.0
Specimen holder model: GATAN LIQUID NITROGEN
Alignment procedure: LEGACY (Astigmatism: Objective lens astigmatism was corrected at 150,000 times magnification, Electron beam tilt params: )
Temperature
Average: 90 K
Image Recording [1]
Detector category: CCD
Detector model: GATAN ULTRASCAN 4000 (4k x 4k)
Number of real images: 38
Average electron dose per image: 18 e/Å2
Image processing [1]
Details: The particles were selected along individual microtubules.
Final reconstruction
Resolution: 20.0 Å ( BY AUTHOR)
Resolution method: OTHER
Number of images used: 2308
Details: Approximately 30,000 asymmetric units were averaged in the final reconstruction.
⌯ Applied Symmetry
Point group: C1
Software [1]
Name Version Details
SPIDER, FREALIGN - -
CTF correction
Details:FREALIGN
Map
Format: CCP4
Data type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation details: Reconstruction of microtubule-bound human kinesin-5 motor domain in presence of ADP and with a glod cluster covalently attached to the residue V365C
Details: ::::EMDATABANK.org::::EMD-2539::::
⬡ Geometry
X Y Z
Dimensions 50 50 50
Origin 122 49 108
Spacing 50 50 50
Voxel size 2.2 Å 2.2 Å 2.2 Å
Contour list
Primary Level Source
True 0.6 AUTHOR