Paper
30 December 2003 Convergent beam neutron crystallography
Walter M. Gibson, Arthur J. Schultz, James W. Richardson, John M. Carpenter, David F. R. Mildner, Heather H. Chen-Mayer, M. E. Miller, E. Maxey, Henry J. Prask, Thomas H. Gnaeupel-Herold, Russell Youngman
Author Affiliations +
Abstract
Applications of neutron diffraction for small samples (<1mm3) or small fiducial areas are limited by the available neutron flux density. Recent demonstrations of convergent beam electron and x-ray diffraction and focusing of cold (λ>1 Å) neutrons suggest the possibility to use convergent beam neutron diffraction for small sample crystallography. We have carried out a systematic study of diffraction of both monoenergetic and broad bandwidth neutrons at the NIST Research Reactor and at the Intense Pulsed Neutron Source (IPNS) at Argonne National Laboratory. Combining convergent beams with time-of-flight Laue diffraction is particularly attractive for high efficiency small sample diffraction studies. We have studied single crystal and powder diffraction of neutrons with convergence angles as large as 15° and have observed diffracted peak intensity gains greater than 20. The convergent beam method (CBM) shows promise for crystallography on small samples of small to medium size molecules (potentially even for proteins), ultra-high pressure samples, and for mapping of strain and texture distributions in larger samples.
© (2003) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Walter M. Gibson, Arthur J. Schultz, James W. Richardson, John M. Carpenter, David F. R. Mildner, Heather H. Chen-Mayer, M. E. Miller, E. Maxey, Henry J. Prask, Thomas H. Gnaeupel-Herold, and Russell Youngman "Convergent beam neutron crystallography", Proc. SPIE 5199, Penetrating Radiation Systems and Applications V, (30 December 2003); https://doi.org/10.1117/12.510736
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KEYWORDS
Diffraction

Crystals

Sensors

Crystallography

Single crystal X-ray diffraction

Laser crystals

Proteins

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