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. 1997 May;72(5):2357–2364. doi: 10.1016/S0006-3495(97)78880-5

Molecular resolution imaging of macromolecular crystals by atomic force microscopy.

Kuznetsov YuG 1, A J Malkin 1, T A Land 1, J J DeYoreo 1, A P Barba 1, J Konnert 1, A McPherson 1
PMCID: PMC1184431  PMID: 9129839

Abstract

Atomic force microscopy (AFM) images at the molecular level have been obtained for a number of different protein and virus crystals. They can be utilized in some special cases to obtain information useful to crystal structure analyses by x-ray diffraction. In particular, questions of space group enantiomer, the packing of molecules within a unit cell, the number of molecules per asymmetric unit, and the dispositions of multiple molecules within the asymmetric unit may be resolved. In addition, because of the increasing sensitivity and resolution of the AFM technique, some molecular features of very large asymmetric units may be within reach. We describe here high-resolution studies, using AFM, to visualize individual molecules and viruses in their crystal lattices. These investigations included fungal lipase, lysozyme, thaumatin, canavalin, and satellite tobacco mosaic virus (STMV).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Derewenda Z. S., Derewenda U., Dodson G. G. The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 A resolution. J Mol Biol. 1992 Oct 5;227(3):818–839. doi: 10.1016/0022-2836(92)90225-9. [DOI] [PubMed] [Google Scholar]
  2. Hardt S., Wang B., Schmid M. F. A brief description of I.C.E.: the integrated crystallographic environment. J Struct Biol. 1996 Jan-Feb;116(1):68–70. doi: 10.1006/jsbi.1996.0012. [DOI] [PubMed] [Google Scholar]
  3. Ko T. P., Day J., Greenwood A., McPherson A. Structures of three crystal forms of the sweet protein thaumatin. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):813–825. doi: 10.1107/S0907444994005512. [DOI] [PubMed] [Google Scholar]
  4. Ko T. P., Ng J. D., McPherson A. The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). Plant Physiol. 1993 Mar;101(3):729–744. doi: 10.1104/pp.101.3.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Konnert J. H., D'Antonio P., Ward K. B. Observation of growth steps, spiral dislocations and molecular packing on the surface of lysozyme crystals with the atomic force microscope. Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):603–613. doi: 10.1107/S0907444994001988. [DOI] [PubMed] [Google Scholar]
  6. Koszelak S., Dodds J. A., McPherson A. Preliminary analysis of crystals of satellite tobacco mosaic virus. J Mol Biol. 1989 Sep 20;209(2):323–325. doi: 10.1016/0022-2836(89)90281-7. [DOI] [PubMed] [Google Scholar]
  7. Land TA, Malkin AJ, Kuznetsov YG, McPherson A, De Yoreo JJ Mechanisms of protein crystal growth: An atomic force microscopy study of canavalin crystallization. Phys Rev Lett. 1995 Oct 2;75(14):2774–2777. doi: 10.1103/PhysRevLett.75.2774. [DOI] [PubMed] [Google Scholar]
  8. Larson S. B., Koszelak S., Day J., Greenwood A., Dodds J. A., McPherson A. Three-dimensional structure of satellite tobacco mosaic virus at 2.9 A resolution. J Mol Biol. 1993 May 20;231(2):375–391. doi: 10.1006/jmbi.1993.1289. [DOI] [PubMed] [Google Scholar]
  9. Malkin A. J., Kuznetsov YuG, Land T. A., DeYoreo J. J., McPherson A. Mechanisms of growth for protein and virus crystals. Nat Struct Biol. 1995 Nov;2(11):956–959. doi: 10.1038/nsb1195-956. [DOI] [PubMed] [Google Scholar]
  10. Malkin A. J., Kuznetsov Y. G., McPherson A. Incorporation of microcrystals by growing protein and virus crystals. Proteins. 1996 Feb;24(2):247–252. doi: 10.1002/(SICI)1097-0134(199602)24:2<247::AID-PROT11>3.0.CO;2-N. [DOI] [PubMed] [Google Scholar]
  11. Malkin AJ, Land TA, Kuznetsov YG, McPherson A, DeYoreo JJ. Investigation of virus crystal growth mechanisms by in situ atomic force microscopy. Phys Rev Lett. 1995 Oct 2;75(14):2778–2781. doi: 10.1103/PhysRevLett.75.2778. [DOI] [PubMed] [Google Scholar]
  12. Matthews B. W. Solvent content of protein crystals. J Mol Biol. 1968 Apr 28;33(2):491–497. doi: 10.1016/0022-2836(68)90205-2. [DOI] [PubMed] [Google Scholar]
  13. Ng J. D., Ko T. P., McPherson A. Cloning, expression, and crystallization of jack bean (Canavalia ensiformis) canavalin. Plant Physiol. 1993 Mar;101(3):713–728. doi: 10.1104/pp.101.3.713. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Yip C. M., Ward M. D. Atomic force microscopy of insulin single crystals: direct visualization of molecules and crystal growth. Biophys J. 1996 Aug;71(2):1071–1078. doi: 10.1016/S0006-3495(96)79307-4. [DOI] [PMC free article] [PubMed] [Google Scholar]

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