Electron diffraction from laser-aligned beams of large hydrated molecules

Research output: Contribution to journalArticle

2 Scopus citations

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 languageEnglish (US)
Pages (from-to)163-168
Number of pages6
JournalJournal of Electron Microscopy
Volume54
Issue number3
DOIs
StatePublished - Jun 1 2005

Keywords

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

ASJC Scopus subject areas

  • Instrumentation

Fingerprint Dive into the research topics of 'Electron diffraction from laser-aligned beams of large hydrated molecules'. Together they form a unique fingerprint.

  • Cite this