Electron diffraction from laser-aligned beams of large hydrated molecules

John Spence

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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 languageEnglish (US)
Pages (from-to)163-168
Number of pages6
JournalJournal of Electron Microscopy
Issue number3
StatePublished - Jun 2005


  • Laser-alignment
  • droplet beam
  • protein beam
  • protein diffraction

ASJC Scopus subject areas

  • Instrumentation


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