Neutron Diffraction

  • Hans Frauenfelder
Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)


X-rays are scattered by atomic electrons, neutrons by atomic nuclei. The two techniques are not in competition; they are complementary. Because neutron sources are many orders of magnitude weaker than X-ray sources, it is likely that neutron scattering will not be used for routine structure determination but will be important for the determination of the position of the crucial hydrogen atoms. The following discussion is brief; details can be found in a number of books, reviews, and papers [1]–[5].


Atomic Nucleus Neutron Scattering Neutron Source Nuclear Force Atomic Electron 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    G. E. Bacon. Neutron Diffraction, 3rd edition. Clarendon, Oxford, 1975.Google Scholar
  2. 2.
    A. A. Kossiakoff. Neutron protein crystallography. Ann. Rev. Biophys. Bioeng., 12:159–82, 1983.CrossRefGoogle Scholar
  3. 3.
    B. P. Schoenborn and R. B. Knott, editors. Neutrons in Biology. Plenum Press, New York, 1996.Google Scholar
  4. 4.
    H. B. Stuhrmann. Unique aspects of neutron scattering for the study of biological systems. Rep. Prog. Phys., 67:1073–1115, 2004.ADSCrossRefGoogle Scholar
  5. 5.
    B. P. Schoenborn and R. Knott. Neutron sources. In M. G. Rossmann and E. Arnold, editors, International Tables for Crystallography, Vol. F, Chapter 6.2. Kluwer Acad. Publishers, Dordrecht, 2001, pp. 133–142.Google Scholar
  6. 6.
    P. Langan, G. Greene, and B. P. Schoenborn. Protein crystallography with spallation neutrons:The user facility at Los Alamos Neutron Science Center. J. Appl. Crystallography, 37:24–31, 2004.CrossRefGoogle Scholar
  7. 7.
    F. Shu, V. Ramakrishnan, and B. P. Schoenborn. Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin. Proc. Natl. Acad. Sci. USA, 97:3827–77, 2000.Google Scholar
  8. 8.
    T. Chatake, A. Ostermann, K. Kurihara, F. G. Parak, and N. Niimura. Hydration in proteins observed by high-resolution neutron crystallography. Proteins: Structure, Function, and Bioinformatics, 50:516–23, 2003.CrossRefGoogle Scholar
  9. 9.
    M. P. Blakeley, A. J. Kalb (Gilboa), J. R. Helliwell, and D. A. A. Myles. The 15–The 15–K neutron structure of saccaride-free concavalin a. Proc. Natl. Acad. Sci. USA, 101:16405–10, 2004.ADSCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Hans Frauenfelder
    • 1
  1. 1.Theory DivisionLos Alamos National LaboratoryLos AlamosUSA

Personalised recommendations