Fundamentals of Neutron Diffraction

  • V. Ramakrishnan
Part of the NATO ASI Series book series (NSSA, volume 183)


The purpose of this article is to describe the differences between neutron diffraction and X-ray diffraction, and to give specific examples of how these differences have been exploited in the study of biological structures. Those who wish a comprehensive treatment of this topic can turn to a number of reviews and symposium volumes that deal with the application of neutron scattering to biological problems (Schoenborn and Nunes, 1972; Engelman and Moore, 1975; Jacrot, 1976; Kneale et al., 1977; Moore, 1982; Schoenborn, 1984).


Neutron Diffraction Neutron Scattering Neutron Beam Biological Macromolecule Brookhaven National Laboratory 
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. Bacon, G.E., 1975, Neutron Diffraction, Clarendon Press, Oxford.Google Scholar
  2. Bragg, W.L. and Perutz, M.F., 1952, The external form of the haemoglobin molecule, Acta Crystallogr. 5:277.CrossRefGoogle Scholar
  3. Capel, M.S., Engelman, D.M., Freeborn, B.R., Kjeldgaard, M., Langer, J.A., Ramakrishnan, V., Schindler, D.G., Schneider, D.K., Schoenborn, B.P., Sillers, L-Y., Yabuki, S. and Moore, P.B., 1987, A complete mapping of the positions of the proteins in the small ribosomal subunit of E. coli, Science 238:1327.CrossRefGoogle Scholar
  4. Debye, P., 1915, Zerstreuung von Röntgenstrahlen, Ann. Phys. 46:809.CrossRefGoogle Scholar
  5. Doster, W., Cusack, S. and Perry, W., 1989, Dynamical transition of myoglobin revealed by inelastic neutron scattering, Nature 337:754.ADSCrossRefGoogle Scholar
  6. Cheng, X. and Schoenborn, B.P., 1989, Hydration in protein crystals, Acta Crystallogr., in press.Google Scholar
  7. Engelman, D.M. and Moore, P.B., 1972, A new method for the determination of biological quaternary structures by neutron scattering, Proc. Natl. Acad. Sci. USA 69:1997.ADSCrossRefGoogle Scholar
  8. Engelman, D.M. and Moore, P.B., 1975, Determination of quaternary structure by small angle neutron scattering, Ann. Rev. Biophys. Bioeng. 4:219.CrossRefGoogle Scholar
  9. Guinier, A. and Fournet, G., 1955, “Small angle scattering of X-rays,” Wiley, New York.Google Scholar
  10. Hjelm, R.P., Kneale, G.G., Suau, P., Baldwin, J.P., Bradbury, E.M. and Ibel, K., 1977, Small angle neutron scattering studies of chromatin subunits in solution, Cell 10:139.CrossRefGoogle Scholar
  11. Ibel, K. and Stuhrmann, H.B., 1975, Comparison of neutron and X-ray scattering of dilute myoglobin solutions, J. Mol. Biol. 93:255.CrossRefGoogle Scholar
  12. Jacrot, B., 1976, The study of biological structures by neutron scattering from solution, Rep. Prog. Phys. 39:911.ADSCrossRefGoogle Scholar
  13. Kneale, G.G., Baldwin, J.P. and Bradbury, E.M., 1977, Neutron scattering studies of biological macromolecules in solution, Q. Rev. Biophys. 10:485.CrossRefGoogle Scholar
  14. Kossiakoff, A.A., 1982, Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique, Nature 296:713.ADSCrossRefGoogle Scholar
  15. Kossiakoff, A.A. and Shteyn, S., 1984, Effect of packing structure on side-chain methyl rotor conformations, Nature 311:582.ADSCrossRefGoogle Scholar
  16. Kossiakoff, A.A. and Spencer, S.A., 1980, Neutron diffraction identifies His-57 as the catalytic base in trypsin, Nature 288:414.ADSCrossRefGoogle Scholar
  17. Kossiakoff, A.A. and Spencer, S.A., 1981, Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of serine proteases: neutron structure of trypsin, Biochemistry 20:6462.CrossRefGoogle Scholar
  18. Moore, P.B., 1982, Small angle scattering techniques for the study of biological macromolecules and macromolecular aggregates, Meth. Exp. Phys. 20:3370.Google Scholar
  19. Moore, P.B. and Weinstein, E., 1979, On the estimation of the locations of subunits within macromolecular aggregates from neutron interference data, J. Appl. Cryst. 12:321.CrossRefGoogle Scholar
  20. Novotny, V., May, R.P. and Nierhaus, K.H., 1986, in: “Structure, Function and Genetics of Ribosomes,” Hardesty, B. and Kramer, G., eds., Springer-Verlag, Berlin.Google Scholar
  21. Pardon, J.F., Worcester, D.L., Wooley, J.C., Tatchell, K., Van Holde, K.E. and Richards, B.M., 1975, Low angle neutron scattering from chromatin subunit particles, Nucl. Acids Res. 2:2163.CrossRefGoogle Scholar
  22. Schoenborn, B.P. and Nunes, A.C., 1972, Neutron Diffraction, Ann. Rev. Biophys. Bioeng. 1:529.CrossRefGoogle Scholar
  23. Schoenborn, B.P., ed., 1975, “Neutron scattering for the analysis of biological structures,” Brookhaven Symposia in Biology, volume 27, U.S. Government Printing Office.Google Scholar
  24. Schoenborn, B.P., ed., 1984, “Neutrons in Biology,” Plenum Press, New York.Google Scholar
  25. Stuhrmann, H.B., 1974, Neutron small angle scattering of biological macromolecules in solution, J. Appl. Cryst. 7:173.CrossRefGoogle Scholar
  26. Teeter, M. and Kossiakoff, A.A., 1984, The neutron structure of the hydrophobic plant protein crambin, in: “Neutrons in Biology,” Schoenborn, B.P., ed., Plenum Press, New York.Google Scholar
  27. Wittmann, H.G., 1982, Components of Bacterial Ribosomes, Ann. Rev. Biochem. 51:155.CrossRefGoogle Scholar
  28. Wlodawer, A. and Sjolin, L., 1984, Application of joint neutron and X-ray refinement to t he investigation of the structure of ribonuclease A at 2.0 Å resolution, in: “Neutrons in Biology,” Schoenborn, B.P. ed., Plenum Press, New York.Google Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • V. Ramakrishnan
    • 1
  1. 1.Biology DepartmentBrookhaven National LaboratoryUptonUSA

Personalised recommendations