EMD-7493

Electron Crystallography
2.8 Å
EMD-7493
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Deposition: 02/03/2018
Map released: 16/05/2018
Last modified: 16/10/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-7493
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3D volume (map.gz) Experimental metadata (xml) Experimental Metadata (cif.gz)
Map-only Validation report (pdf.gz) Map-only Validation report (cif.gz) Map-only Validation report (xml.gz)
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EMICSS annotations (xml)

2.80 A MicroED structure of proteinase K at 6.0 e- / A^2

EMD-7493

Electron Crystallography
2.8 Å
EMD-7493
3D View Gallery
Deposition: 02/03/2018
Map released: 16/05/2018
Last modified: 16/10/2024
Overview 3D View Sample Experiment Validation Additional data Links
Method: Electron Crystallography
Aggregation State: 3D Array
Specimen preparation [1]
Concentration: 25 mg/mL
Buffer
pH: 8.0
Buffer components [2]:
Name Formula Concentration ChEBI
Ammonium sulfate N2H8SO4 1.2 M
Tris C4H11NO3 0.1 M
Vitrification
Cryogen name: ETHANE
Chamber humidity: 30%
Instrument: FEI VITROBOT MARK IV
Microscopy [1]
Microscope: FEI TECNAI F20
Illumination mode: FLOOD BEAM
Imaging mode: DIFFRACTION
Electron source: FIELD EMISSION GUN
Acceleration voltage: 200 kV
Camera Length: 1200 mm
Cooling holder cryogen: NITROGEN
Image Recording [1]
Detector model: TVIPS TEMCAM-F416 (4k x 4k)
Dimensions: 2048 pixel x 2048 pixel
Number of grids: 1
Number of real images: 240
Number of diffraction images: 240
Average exposure time: 5.1 s
Average electron dose per image: 0.0357 e/Å2
Image processing [1]
Final reconstruction
Resolution: 2.8 Å ( BY AUTHOR)
Resolution method: DIFFRACTION PATTERN/LAYERLINES
Molecular replacement
Software [1]
Name Version Details
MOLREP 11.4.05 -
⌯ Symmetry determination
Software [1]
Name Version Details
POINTLESS 1.11.3 -
Merging
Software [1]
Name Version Details
AIMLESS 0.5.32 -
Crystallography statistics
Number of intensities measured: 30596
Number of structure factors: 5423
Fourier space coverage: 88.4
R sym: 0.536
R merge: 0.536
Overall phase error: 62.59
Overall phase residual: 62.59
Phase error rejection criteria: 0
High resolution: 2.8 Å
Shell list [1]
High resolution Low resolution Number of structure factors Phase residual Fourier space coverage Multiplicity
2.8 Å 2.87 Å 374 71.28 88.21 5.8
Map
Format: CCP4
Data type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation details: 2.80 A MicroED density map of proteinase K at 6.0 e- / A^2
⬡ Geometry
X Y Z
Origin -47 -5 -31
Dimensions (px) 58 54 62
Dimensions (Å) 67.4502 67.4502 100.8179
Voxel size (Å) 0.93680835 0.93680835 0.90015984
Contour list
Primary Level Source
True 0.19626 AUTHOR