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Diffraction and imaging from a beam of laser‐aligned proteins: resolution limits

Diffraction and imaging from a beam of laser‐aligned proteins: resolution limits The effect of the limited alignment of hydrated molecules is considered in a laser‐aligned molecular beam, on diffraction patterns taken from the beam. Simulated patterns for a protein beam are inverted using the Fienup–Gerchberg–Saxton phasing algorithm, and the effect of limited alignment on the resolution of the resulting potential maps is studied. For a typical protein molecule (lysozyme) with anisotropic polarizability, it is found that up to 1 kW of continuous‐wave near‐infrared laser power (depending on dielectric constant), together with cooling to liquid‐nitrogen temperatures, may be needed to produce sufficiently accurate alignment for direct observation of the secondary structure of proteins in the reconstructed potential or charge‐density map. For a typical virus (TMV), a 50 W continuous‐wave laser is adequate for subnanometre resolution at room temperature. The dependence of resolution on laser power, temperature, molecular size, shape and dielectric constant is analyzed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section A Foundations of Crystallography Wiley

Diffraction and imaging from a beam of laser‐aligned proteins: resolution limits

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References (18)

Publisher
Wiley
Copyright
Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0108-7673
eISSN
1600-5724
DOI
10.1107/S0108767305002710
pmid
15724074
Publisher site
See Article on Publisher Site

Abstract

The effect of the limited alignment of hydrated molecules is considered in a laser‐aligned molecular beam, on diffraction patterns taken from the beam. Simulated patterns for a protein beam are inverted using the Fienup–Gerchberg–Saxton phasing algorithm, and the effect of limited alignment on the resolution of the resulting potential maps is studied. For a typical protein molecule (lysozyme) with anisotropic polarizability, it is found that up to 1 kW of continuous‐wave near‐infrared laser power (depending on dielectric constant), together with cooling to liquid‐nitrogen temperatures, may be needed to produce sufficiently accurate alignment for direct observation of the secondary structure of proteins in the reconstructed potential or charge‐density map. For a typical virus (TMV), a 50 W continuous‐wave laser is adequate for subnanometre resolution at room temperature. The dependence of resolution on laser power, temperature, molecular size, shape and dielectric constant is analyzed.

Journal

Acta Crystallographica Section A Foundations of CrystallographyWiley

Published: Mar 1, 2005

Keywords: ;

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