Journal:Acta Cryst D:S2059798320014540
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
Electron crystallography employs standard transmission electron microscopes as opposed to large-scale facilities for X-ray or neutron. It is also more sensitive to atomic charges, which are important for understanding enzyme catalysis and other protein functions. Besides, only nanosized crystals are required. Nevertheless, the strong interaction with matter means that electron multiple scattering is non-negligible, which complicates structure determination. | Electron crystallography employs standard transmission electron microscopes as opposed to large-scale facilities for X-ray or neutron. It is also more sensitive to atomic charges, which are important for understanding enzyme catalysis and other protein functions. Besides, only nanosized crystals are required. Nevertheless, the strong interaction with matter means that electron multiple scattering is non-negligible, which complicates structure determination. | ||
| - | Taking into consideration the effect of multiple scattering, we correct the diffraction intensities using a likelihood-based algorithm. As shown in the figures (Figure 2 and Figure 4 in the manuscript), this method has improved the resulting structure and has permitted us to estimate the charge of the Zn ion in the thermolysin and insulin crystals. | + | Taking into consideration the effect of multiple scattering, we correct the diffraction intensities using a likelihood-based algorithm. As shown in the figures (Figure 2 and Figure 4 in the manuscript), this method has improved the resulting structure and has permitted us to estimate the charge of the Zn ion in the thermolysin and insulin crystals. <scene name='86/868205/Cv1/1'>TextToBeDisplayed</scene> |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 07:14, 25 November 2020
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