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Growth kinetics and diffraction properties of STMV crystals

Published online by Cambridge University Press:  14 March 2011

Yu. G. Kuznetsov
Affiliation:
University of California, Irvine Department of Molecular Biology and Biochemistry Irvine, CA 92697-3900
A. J. Malkin
Affiliation:
University of California, Irvine Department of Molecular Biology and Biochemistry Irvine, CA 92697-3900
A. McPherson
Affiliation:
University of California, Irvine Department of Molecular Biology and Biochemistry Irvine, CA 92697-3900
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Abstract

Two crystal forms, orthorhombic and cubic, of satellite tobacco mosaic virus have been investigated. Atomic force microscopy showed that the orthorhombic crystals were characterized by a high density of point defects, while the cubic crystals were practically defect-free. Nonetheless, orthorhombic crystals diffract to a high resolution of 1.8 Å while the cubic crystals diffract to only about 4 to 6 Å resolution. Differences in the properties of viruses incorporated into the two crystal structures were demonstrated by growth kinetics studies. It appears that physical and chemical treatments applied to protein and virus solutions during their extraction and purification introduce a variety of specific structural changes and that these alterations may then affect the diffraction properties of resultant macromolecular crystals.

Type
Research Article
Copyright
Copyright © Materials Research Society 2000

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References

REFERENCES

1. Wiencek, J. M. and Jones, W. F., Abstracts of the 8th International Conference on the Crystallization of Biological Macromolecules, May 14-19, 2000, Sandestin, Florida (USA), p. 40.Google Scholar
2. McPherson, A., Crystallogr. Rev. 6, 157308 (1996).Google Scholar
3. Thomas, B. R., Vekilovand, P. G. Rosenberger, F., Acta Cryst. Sec D, 52, 776789 (1996).Google Scholar
4. Caylor, C. L., Dobrianov, I., Lemay, S. G., Kimmer, C., Kriminski, S., Finkelstein, K. D., Zipfel, W., Webb, W.W., Tomas, B. R., Chernov, A. A., Thorn, R. E., Proteins-Struct. Func. and Gen. 36, 270281 (1999)Google Scholar
5. Valverde, R. A., Dodds, J. A., J. Gen. Virol. 68, 965972 (1987).Google Scholar
6. Larson, S. B., Koszelak, S., Day, J., Greenwood, A., Dodds, J. A., McPherson, A., Nature 361, 179 (1993).Google Scholar
7. Larson, S. B., Day, J., Greenwood, A. and McPherson, A., J. Mol. Biol. 277, 3759 (1998).Google Scholar
8. Israelachvili, J., Intermolecular & Surface Forces, 2nd ed. (Academic Press, San Diego, 1992), p.246.Google Scholar
9. Malkin, A. J., Kuznetsov, Yu. G., and McPherson, A.,J. Struct. Biol. 117, 124137 (1996).Google Scholar