Electron diffraction from laser-aligned beams of large hydrated molecules

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 2005

Fingerprint

Electron diffraction
Diffraction patterns
Laser beams
Lasers
diffraction patterns
electron diffraction
Electrons
proteins
Proteins
Secondary Protein Structure
Molecules
Molecular beams
Infrared lasers
Charge density
infrared lasers
molecular beams
lasers
molecules
Hot Temperature
alignment

Keywords

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

ASJC Scopus subject areas

  • Instrumentation

Cite this

Electron diffraction from laser-aligned beams of large hydrated molecules. / Spence, John.

In: Journal of Electron Microscopy, Vol. 54, No. 3, 06.2005, p. 163-168.

Research output: Contribution to journalArticle

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