Abstract
The principal aim in the determination of protein structure by using neutron diffraction is to find the positions of hydrogen atoms. Since protein crystals used in neutron investigations are usually deuterated (in order to decrease the incoherent scattering by hydrogen atoms), it is also possible to identify highly protected main-chain amide groups (10, 24). While in principle it is possible to determine the neutron structure of a protein de novo, by using either isomorphous replacement with isotopes such as 164Dy or anomalous scattering of 113Cd, 149Sm, or 157Gd, such attempts have not progressed beyond the testing of their feasibility (17). All neutron structures completed to date have utilized x-ray models in the initial stages of the investigation in order to provide the starting set of phases. In most cases the x-ray coordinates were not used after this initial step, and the neutron refinement proceeded on its own (2, 7, 11, 14). On the other hand, Wlodawer and Hendrickson (23) proposed a method of refinement in which the structure is jointly refined with the neutron and x-ray data. In this report we will describe our experience with the application of joint refinement to the determination of the structure of ribonuclease A at 2.0-Å resolution, and we will discuss the validity of this procedure.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Bentley, G.A., Duee, E.D., Mason, S.A., and Nunes, A.C., J. Chim. Phys. 76:817 (1979).
Bentley, G.A. and Mason, S.A., in: “Structural Studies on Molecules of Biological Interest,” G. Dodson et al., eds., p. 246, Clarendon Press, Oxford (1981).
Bundi, A. and Wüthrich, K., Biopolymers 18:285 (1979).
Borkakoti, N., Moss, D.A., and Palmer, R.A., Acta Crystallogr. B38:2210 (1982).
Coppens, P., Boehme, R., Prince, P.F., and Stevens, E.D., Acta Crystallogr. A37:857 (1981).
Glasoe, P.K. and Long, F.A., J. Phys. Chem. 64:188, (1960).
Hanson, J. and Schoenborn, B.P., J. Mol. Biol. 153:117 (1981).
Hendrickson, W.A. and Konnert, J.H., in: “Biomolecular Structure, Conformation, Function, and Evolution,” R. Srinivasan, ed., Vol. 1, p. 43, Pergamon, Oxford (1981).
Hoppe, W., Brookhaven Symp. Biol. 27:11–22 (1976).
Kossiakoff, A.A., Nature (London) 296:713 (1982).
Kossiakoff, A.A. and Spencer, S.A., Biochemistry 20:6462 (1981).
Luzzati, V., Acta Crystallogr. 5:802 (1952).
Phillips, S.E.V., J. Mol. Biol. 142:531 (1980).
Phillips, S.E.V. and Schoenborn, B. P., Nature (London) 292:81 (1981).
Prince, E., Wlodawer, A., and Santoro, A., J. Appl. Crystallogr. 11:173 (1978).
Roberts, G.C.K., Meadows, D.H., and Jardetzky, O., Biochemistry 8:2053 (1969).
Schoenborn, B.P., in: “Anomalous Scattering,” S. Ramaseshan and S.C. Abrahams, eds., p. 407, Munksgaard, Copenhagen (1975).
Sjölin, L. and Wlodawer, A., Acta Crystallogr. A37:594 (1981).
Takano, T., J. Mol. Biol. 110:537 (1977).
Wlodawer, A., Acta Crystallogr. B36:1826 (1980).
Wlodawer, A. and Sjölin, L., Proc. Natl. Acad. Sci USA 78:2853 (1981).
Wlodawer, A., Bott, R. and Sjölin, L., J. Biol. Chem. 257:1325 (1982).
Wlodawer, A. and Hendrickson, W.A., Acta Crystallogr. A38:239 (1982).
Wlodawer, A. and Sjölin, L., Proc. Natl. Acad. Sci. USA 79:1418 (1982).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1984 Springer Science+Business Media New York
About this chapter
Cite this chapter
Wlodawer, A., Sjölin, L. (1984). Application of Joint Neutron and X-Ray Refinement to the Investigation of the Structure of Ribonuclease A at 2.0-Å Resolution. In: Schoenborn, B.P. (eds) Neutrons in Biology. Basic Life Sciences, vol 27. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0375-4_21
Download citation
DOI: https://doi.org/10.1007/978-1-4899-0375-4_21
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-0377-8
Online ISBN: 978-1-4899-0375-4
eBook Packages: Springer Book Archive