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diffraction grating replica with amorphous gold shadowing  (Ted Pella)

 
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    Ted Pella diffraction grating replica with amorphous gold shadowing
    Electron-counting MicroED data of proteinase K using the K2 camera. (A) <t>Diffraction</t> pattern of a proteinase K crystal recorded using the K2 in electron counting mode, showing spots to beyond 2.5 Å resolution. For display, frames are cropped around the area of interest and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.3° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.
    Diffraction Grating Replica With Amorphous Gold Shadowing, supplied by Ted Pella, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/diffraction+grating+replica+with+amorphous+gold+shadowing/pmc09999727-96-10-17?v=Ted+Pella
    Average 90 stars, based on 1 article reviews
    diffraction grating replica with amorphous gold shadowing - by Bioz Stars, 2026-07
    90/100 stars

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    1) Product Images from "Electron-counting MicroED data with the K2 and K3 direct electron detectors"

    Article Title: Electron-counting MicroED data with the K2 and K3 direct electron detectors

    Journal: Journal of structural biology

    doi: 10.1016/j.jsb.2022.107886

    Electron-counting MicroED data of proteinase K using the K2 camera. (A) Diffraction pattern of a proteinase K crystal recorded using the K2 in electron counting mode, showing spots to beyond 2.5 Å resolution. For display, frames are cropped around the area of interest and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.3° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.
    Figure Legend Snippet: Electron-counting MicroED data of proteinase K using the K2 camera. (A) Diffraction pattern of a proteinase K crystal recorded using the K2 in electron counting mode, showing spots to beyond 2.5 Å resolution. For display, frames are cropped around the area of interest and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.3° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Techniques Used: Comparison

    Electron-counting MicroED data of proteinase K using the K3 camera without a beam stop. (A) Diffraction pattern of a proteinase K lamella recorded using the K3 in electron counting mode, showing spots up to 1.7 Å resolution. For display, frames are cropped around the area of interest at the diffraction limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.
    Figure Legend Snippet: Electron-counting MicroED data of proteinase K using the K3 camera without a beam stop. (A) Diffraction pattern of a proteinase K lamella recorded using the K3 in electron counting mode, showing spots up to 1.7 Å resolution. For display, frames are cropped around the area of interest at the diffraction limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Techniques Used: Comparison

    Electron-counting MicroED data of triclinic lysozyme using the K3 camera without beam stop. (A) Diffraction pattern of a lysozyme lamella recorded using the K3 in electron counting mode, showing spots to beyond 1.2 Å resolution. For display, frames are cropped around the area of interest at the resolution limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The map shown for a slice through the structural model as indicated by the inset. The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.
    Figure Legend Snippet: Electron-counting MicroED data of triclinic lysozyme using the K3 camera without beam stop. (A) Diffraction pattern of a lysozyme lamella recorded using the K3 in electron counting mode, showing spots to beyond 1.2 Å resolution. For display, frames are cropped around the area of interest at the resolution limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The map shown for a slice through the structural model as indicated by the inset. The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Techniques Used:



    Similar Products

    diffraction grating replica with amorphous gold shadowing  (Ted Pella)
    90
    Ted Pella diffraction grating replica with amorphous gold shadowing
    Electron-counting MicroED data of proteinase K using the K2 camera. (A) <t>Diffraction</t> pattern of a proteinase K crystal recorded using the K2 in electron counting mode, showing spots to beyond 2.5 Å resolution. For display, frames are cropped around the area of interest and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.3° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.
    Diffraction Grating Replica With Amorphous Gold Shadowing, supplied by Ted Pella, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/diffraction+grating+replica+with+amorphous+gold+shadowing/pmc09999727-96-10-17?v=Ted+Pella
    Average 90 stars, based on 1 article reviews
    diffraction grating replica with amorphous gold shadowing - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Electron-counting MicroED data of proteinase K using the K2 camera. (A) Diffraction pattern of a proteinase K crystal recorded using the K2 in electron counting mode, showing spots to beyond 2.5 Å resolution. For display, frames are cropped around the area of interest and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.3° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Journal: Journal of structural biology

    Article Title: Electron-counting MicroED data with the K2 and K3 direct electron detectors

    doi: 10.1016/j.jsb.2022.107886

    Figure Lengend Snippet: Electron-counting MicroED data of proteinase K using the K2 camera. (A) Diffraction pattern of a proteinase K crystal recorded using the K2 in electron counting mode, showing spots to beyond 2.5 Å resolution. For display, frames are cropped around the area of interest and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.3° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Article Snippet: The sample to detector distance was a calibrated using a diffraction grating replica with amorphous gold shadowing (Ted Pella Inc., product no. 673).

    Techniques: Comparison

    Electron-counting MicroED data of proteinase K using the K3 camera without a beam stop. (A) Diffraction pattern of a proteinase K lamella recorded using the K3 in electron counting mode, showing spots up to 1.7 Å resolution. For display, frames are cropped around the area of interest at the diffraction limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Journal: Journal of structural biology

    Article Title: Electron-counting MicroED data with the K2 and K3 direct electron detectors

    doi: 10.1016/j.jsb.2022.107886

    Figure Lengend Snippet: Electron-counting MicroED data of proteinase K using the K3 camera without a beam stop. (A) Diffraction pattern of a proteinase K lamella recorded using the K3 in electron counting mode, showing spots up to 1.7 Å resolution. For display, frames are cropped around the area of interest at the diffraction limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The refined map shown for a slice through the structural model as indicated by the inset. For comparison, the same slice is shown in . The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Article Snippet: The sample to detector distance was a calibrated using a diffraction grating replica with amorphous gold shadowing (Ted Pella Inc., product no. 673).

    Techniques: Comparison

    Electron-counting MicroED data of triclinic lysozyme using the K3 camera without beam stop. (A) Diffraction pattern of a lysozyme lamella recorded using the K3 in electron counting mode, showing spots to beyond 1.2 Å resolution. For display, frames are cropped around the area of interest at the resolution limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The map shown for a slice through the structural model as indicated by the inset. The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Journal: Journal of structural biology

    Article Title: Electron-counting MicroED data with the K2 and K3 direct electron detectors

    doi: 10.1016/j.jsb.2022.107886

    Figure Lengend Snippet: Electron-counting MicroED data of triclinic lysozyme using the K3 camera without beam stop. (A) Diffraction pattern of a lysozyme lamella recorded using the K3 in electron counting mode, showing spots to beyond 1.2 Å resolution. For display, frames are cropped around the area of interest at the resolution limit and were summed to cover a wedge in reciprocal space of approximately 1.0°. (B) Peak profiles at different resolutions are shown for individual frames used for data integration corresponding to a 0.076° wedge. (C) Plots showing the mean I/σI, CC 1/2 , and data completeness as a function of the resolution for individual crystal datasets and the merged data. The fourth panel shows the correlation coefficient between the observed and calculated structure factor amplitudes for equally sized resolution bins. (D) The map shown for a slice through the structural model as indicated by the inset. The 2mFo-DFc map is shown as blue mesh at a contour level of 1.2σ, the mFo-DFc difference map is contoured at ± 3σ as green and red mesh for positive and negative values, respectively.

    Article Snippet: The sample to detector distance was a calibrated using a diffraction grating replica with amorphous gold shadowing (Ted Pella Inc., product no. 673).

    Techniques: