Tables for
Volume B
Reciprocal space
Edited by U. Shmueli

International Tables for Crystallography (2006). Vol. B, ch. 2.3, pp. 262-263   | 1 | 2 |

Section 2.3.9. Conclusions

M. G. Rossmanna* and E. Arnoldb

aDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA, and  bCABM & Rutgers University, 679 Hoes Lane, Piscataway, New Jersey 08854-5638, USA
Correspondence e-mail:

2.3.9. Conclusions

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Complete interpretation of Patterson maps is no longer used frequently in structure analysis, although most determinations of heavy-atom positions of isomorphous pairs are based on Patterson analyses. Incorporation of the Patterson concept is crucial in many sophisticated techniques essential for the solution of complex problems, particularly in the application to biological macromolecular structures. Patterson techniques provide important physical insights in a link between real- and reciprocal-space formulation of crystal structures and diffraction data. Update

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This article was originally completed in January 1986. Since then, some advances have occurred. In particular, the use of real-space averaging between noncrystallographically related electron density within the crystallographic asymmetric unit has become an accepted way of extending phase information to higher resolution, particularly for complex structures such as viruses (Gaykema et al., 1984[link]; Rossmann et al., 1985[link]; Hogle et al., 1985[link]; Arnold et al., 1987[link]; Hosur et al., 1987[link]; Luo et al., 1987[link]; Acharya et al., 1989[link]). The power of this procedure has been examined theoretically by Arnold & Rossmann (1986)[link].

The availability of fast computers with large random access memories and even larger disk storage also makes many of the techniques considered here commonplace and no longer subject to limitations of computer hardware. For instance, numerous rotation and translation functions can be evaluated rapidly, making it possible to explore many alternative interpretations of such functions in the anticipation that there must be one solution consistent with the available search models and the observed data. Such possibilities have encouraged the creation of powerful computer packages such as MERLOT (Fitzgerald, 1988[link]), BRUTE (Fujinaga & Read, 1987[link]), a package based on a generalized locked rotation function (Tong & Rossmann, 1990[link]) and others. In addition, ab initio phase determination based on noncrystallographic redundancy has become a fairly common event (Rossmann, 1990[link]).


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Arnold, E. & Rossmann, M. G. (1986). Effect of errors, redundancy, and solvent content in the molecular replacement procedure for the structure determination of biological macromolecules. Proc. Natl Acad. Sci. USA, 83, 5489–5493.
Arnold, E., Vriend, G., Luo, M., Griffith, J. P., Kamer, G., Erickson, J. W., Johnson, J. E. & Rossmann, M. G. (1987). The structure determination of a common cold virus, human rhinovirus 14. Acta Cryst. A43, 346–361.
Fitzgerald, P. M. D. (1988). MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Cryst. 21, 273–278.
Fujinaga, M. & Read, R. J. (1987). Experiences with a new translation-function program. J. Appl. Cryst. 20, 517–521.
Gaykema, W. P. J., Hol, W. G. J., Vereijken, J. M., Soeter, N. M., Bak, H. J. & Beintema, J. J. (1984). 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature (London), 309, 23–29.
Hogle, J. M., Chow, M. & Filman, D. J. (1985). Three-dimensional structure of poliovirus at 2.9 Å resolution. Science, 229, 1358–1365.
Hosur, M. V., Schmidt, T., Tucker, R. C., Johnson, J. E., Gallagher, T. M., Selling, B. H. & Rueckert, R. R. (1987). Structure of an insect virus at 3.0 Å resolution. Proteins, 2, 167–176.
Luo, M., Vriend, G., Kamer, G., Minor, I., Arnold, E., Rossmann, M. G., Boege, U., Scraba, D. G., Duke, G. M. & Palmenberg, A. C. (1987). The atomic structure of Mengo virus at 3.0 Å resolution. Science, 235, 182–191.
Rossmann, M. G. (1990). The molecular replacement method. Acta Cryst. A46, 73–82.
Rossmann, M. G., Arnold, E., Erickson, J. W., Frankenberger, E. A., Griffith, J. P., Hecht, H. J., Johnson, J. E., Kamer, G., Luo, M., Mosser, A. G., Rueckert, R. R., Sherry, B. & Vriend, G. (1985). Structure of a human common cold virus and functional relationship to other picornaviruses. Nature (London), 317, 145–153.
Tong, L. & Rossmann, M. G. (1990). The locked rotation function. Acta Cryst. A46, 783–792.

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