Abstract
We consider X-ray or electron diffraction from a molecular beam of hydrated proteins. These are aligned by the polarized field of a powerful continuous infrared laser. The laser power, temperature and molecular size needed to obtain sufficient alignment accuracy for sharp diffraction patterns is estimated using a thermal average, and the resulting Dawson integral compared with the estimate based on equipartition used in our previous work. The conditions determined allow sub-nanometer resolution charge-density maps to be reconstructed from phased diffraction patterns, so that the secondary structure of the proteins can be observed.
Original language | English (US) |
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Pages (from-to) | 163-168 |
Number of pages | 6 |
Journal | Journal of Electron Microscopy |
Volume | 54 |
Issue number | 3 |
DOIs | |
State | Published - Jun 2005 |
Keywords
- Laser-alignment
- droplet beam
- protein beam
- protein diffraction
ASJC Scopus subject areas
- Instrumentation