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Ted Pella c reative c diffraction grating replica
C Reative C Diffraction Grating Replica, supplied by Ted Pella, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/c reative c diffraction grating replica/product/Ted Pella
Average 86 stars, based on 1 article reviews
c reative c diffraction grating replica - by Bioz Stars, 2026-05
86/100 stars

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Ted Pella c reative c diffraction grating replica
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Ted Pella diffraction grating replica
(A) Chemical structure of 1 ; (B) MicroED structure of 1 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative <t>diffraction</t> pattern (658 mm) and crystal appearance (SA 5300x) of 1 under TEM. Scale bar: 2 µm; (D) Packing diagram in 1 , viewed along b ‐ or c ‐ axis. Hydrogen bonding interactions were presented in orange dashed lines.
Diffraction Grating Replica, supplied by Ted Pella, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Ted Pella diffraction calibration grating replica
(A) Chemical structure of 1 ; (B) MicroED structure of 1 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative <t>diffraction</t> pattern (658 mm) and crystal appearance (SA 5300x) of 1 under TEM. Scale bar: 2 µm; (D) Packing diagram in 1 , viewed along b ‐ or c ‐ axis. Hydrogen bonding interactions were presented in orange dashed lines.
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Ted Pella gold diffraction grating replica with latex spheres
(A) Chemical structure of 1 ; (B) MicroED structure of 1 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative <t>diffraction</t> pattern (658 mm) and crystal appearance (SA 5300x) of 1 under TEM. Scale bar: 2 µm; (D) Packing diagram in 1 , viewed along b ‐ or c ‐ axis. Hydrogen bonding interactions were presented in orange dashed lines.
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Ted Pella diffraction grating replica with latex spheres
(A) Chemical structure of 1 ; (B) MicroED structure of 1 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative <t>diffraction</t> pattern (658 mm) and crystal appearance (SA 5300x) of 1 under TEM. Scale bar: 2 µm; (D) Packing diagram in 1 , viewed along b ‐ or c ‐ axis. Hydrogen bonding interactions were presented in orange dashed lines.
Diffraction Grating Replica With Latex Spheres, 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/result/diffraction grating replica with latex spheres/product/Ted Pella
Average 90 stars, based on 1 article reviews
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Ted Pella standard sample diffraction grating replica with latex spheres
(A) Chemical structure of 1 ; (B) MicroED structure of 1 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative <t>diffraction</t> pattern (658 mm) and crystal appearance (SA 5300x) of 1 under TEM. Scale bar: 2 µm; (D) Packing diagram in 1 , viewed along b ‐ or c ‐ axis. Hydrogen bonding interactions were presented in orange dashed lines.
Standard Sample Diffraction Grating Replica With Latex Spheres, 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
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Average 90 stars, based on 1 article reviews
standard sample diffraction grating replica with latex spheres - by Bioz Stars, 2026-05
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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/result/diffraction grating replica with amorphous gold shadowing/product/Ted Pella
Average 90 stars, based on 1 article reviews
diffraction grating replica with amorphous gold shadowing - by Bioz Stars, 2026-05
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Ted Pella diffraction grating replica latex spheres
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 Latex Spheres, 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/result/diffraction grating replica latex spheres/product/Ted Pella
Average 90 stars, based on 1 article reviews
diffraction grating replica latex spheres - by Bioz Stars, 2026-05
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Image Search Results


(A) Chemical structure of 1 ; (B) MicroED structure of 1 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 1 under TEM. Scale bar: 2 µm; (D) Packing diagram in 1 , viewed along b ‐ or c ‐ axis. Hydrogen bonding interactions were presented in orange dashed lines.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 1 ; (B) MicroED structure of 1 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 1 under TEM. Scale bar: 2 µm; (D) Packing diagram in 1 , viewed along b ‐ or c ‐ axis. Hydrogen bonding interactions were presented in orange dashed lines.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques:

(A) Chemical structure of 9 ; (B) MicroED structure of 9 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 9 under TEM. Scale bar: 2 µm; (D) Weak C─H···O hydrogen bonding interaction for one molecule of 9 . (E) Packing diagram in 9 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in blue dashed lines.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 9 ; (B) MicroED structure of 9 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 9 under TEM. Scale bar: 2 µm; (D) Weak C─H···O hydrogen bonding interaction for one molecule of 9 . (E) Packing diagram in 9 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in blue dashed lines.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques:

(A) Chemical structure of 2 ; (B) MicroED structure of 2 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 2 under TEM. Scale bar: 2 µm; (D) Polymorphic structures and packing diagram in 2 , viewed along b ‐axis. Hydrogen bonding interactions were presented in orange dashed lines. Hydrogen atoms not involved in contact were omitted for clarification.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 2 ; (B) MicroED structure of 2 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 2 under TEM. Scale bar: 2 µm; (D) Polymorphic structures and packing diagram in 2 , viewed along b ‐axis. Hydrogen bonding interactions were presented in orange dashed lines. Hydrogen atoms not involved in contact were omitted for clarification.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques: Clarification Assay

(A) Chemical structure of 4 ; (B) MicroED structure of 4 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 4 under TEM. Scale bar: 2 µm; (D) Packing diagram in 4 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in orange dashed lines.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 4 ; (B) MicroED structure of 4 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 4 under TEM. Scale bar: 2 µm; (D) Packing diagram in 4 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in orange dashed lines.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques:

(A) Chemical structure of 5 ; (B) MicroED structure of 5 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 5 under TEM. Scale bar: 2 µm; (D) Packing diagram in 5 , viewed along the a ‐axis. π‐π and hydrogen bonding interactions were presented in orange dashed lines.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 5 ; (B) MicroED structure of 5 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 5 under TEM. Scale bar: 2 µm; (D) Packing diagram in 5 , viewed along the a ‐axis. π‐π and hydrogen bonding interactions were presented in orange dashed lines.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques:

(A) Chemical structure of 6 ; (B) MicroED structure of 6 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 6 under TEM. Scale bar: 2 µm; (D) Packing diagram in 6 , viewed along a ‐ or b ‐axis. Hydrogen bonding interactions were presented in orange dashed lines. π‐π interactions were presented in green dashed lines. Hydrogen atoms not involved in contact were omitted for clarification.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 6 ; (B) MicroED structure of 6 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 6 under TEM. Scale bar: 2 µm; (D) Packing diagram in 6 , viewed along a ‐ or b ‐axis. Hydrogen bonding interactions were presented in orange dashed lines. π‐π interactions were presented in green dashed lines. Hydrogen atoms not involved in contact were omitted for clarification.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques: Clarification Assay

(A) Chemical structure of 7 ; (B) MicroED structure of 7 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 7 under TEM. Scale bar: 2 µm; (D) Packing diagram in 7 , viewed along the a ‐axis. Forms 1 and 2 were presented in purple and yellow, respectively. Hydrogen bonding interactions were presented in blue dashed lines.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 7 ; (B) MicroED structure of 7 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 7 under TEM. Scale bar: 2 µm; (D) Packing diagram in 7 , viewed along the a ‐axis. Forms 1 and 2 were presented in purple and yellow, respectively. Hydrogen bonding interactions were presented in blue dashed lines.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques:

(A) Chemical structure of 8 ; (B) MicroED structure of 8 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 8 under TEM. Scale bar: 2 µm; (D) Packing diagram in 8 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in blue and green dashed lines. Water molecules were colored in purple balls.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 8 ; (B) MicroED structure of 8 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 8 under TEM. Scale bar: 2 µm; (D) Packing diagram in 8 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in blue and green dashed lines. Water molecules were colored in purple balls.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques:

(A) Chemical structure of 3 ; (B) MicroED structure of 3 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 3 under TEM. Scale bar: 2 µm; (D) Packing diagram in 3 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in orange and cyan dashed lines. Molecules were colored by their symmetries.

Journal: Small (Weinheim an Der Bergstrasse, Germany)

Article Title: Rapid Structural Analysis of Natural Products Using MicroED

doi: 10.1002/smll.202511875

Figure Lengend Snippet: (A) Chemical structure of 3 ; (B) MicroED structure of 3 , 2F o ‐F c density map was shown in a blue mesh at 3σ contour level; (C) Representative diffraction pattern (658 mm) and crystal appearance (SA 5300x) of 3 under TEM. Scale bar: 2 µm; (D) Packing diagram in 3 , viewed along the a ‐axis. Hydrogen bonding interactions were presented in orange and cyan dashed lines. Molecules were colored by their symmetries.

Article Snippet: The parallel beam (∼45.2% intensity) was tuned using a 500 nm diffraction grating replica (prod.# 673; Ted Pella, Inc.) and 70 μm objective aperture at the back focal plane.

Techniques:

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: