Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1998 May;74(5):2674–2679. doi: 10.1016/S0006-3495(98)77973-1

Electron crystallographic analysis of two-dimensional streptavidin crystals coordinated to metal-chelated lipid monolayers.

W Frey 1, J Brink 1, W R Schief Jr 1, W Chiu 1, V Vogel 1
PMCID: PMC1299607  PMID: 9591691

Abstract

Coordination of individual histidine residues located on a protein surface to metal-chelated lipid monolayers is a potentially general method for crystallizing proteins in two dimensions. It was shown recently by Brewster angle microscopy (BAM) that the model protein streptavidin binds via its surface histidines to Cu-DOIDA lipid monolayers, and aggregates into regularly shaped domains that have the appearance of crystals. We have used electron microscopy to confirm that the domains are indeed crystalline with lattice parameters similar to those of the same protein crystallized beneath biotinylated lipid monolayers. Although BAM demonstrates that the two-dimensional protein crystals grown via metal chelation are distinct from the biotin-bound crystals in both microscopic shape and thermodynamic behavior, the two crystal types show similar density projections and the same plane group symmetry.

Full Text

The Full Text of this article is available as a PDF (178.6 KB).

Selected References

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

  1. Avila-Sakar A. J., Chiu W. Visualization of beta-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography. Biophys J. 1996 Jan;70(1):57–68. doi: 10.1016/S0006-3495(96)79597-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blankenburg R., Meller P., Ringsdorf H., Salesse C. Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognition. Biochemistry. 1989 Oct 3;28(20):8214–8221. doi: 10.1021/bi00446a037. [DOI] [PubMed] [Google Scholar]
  3. Chiu W., Avila-Sakar A. J., Schmid M. F. Electron crystallography of macromolecular periodic arrays on phospholipid monolayers. Adv Biophys. 1997;34:161–172. doi: 10.1016/s0065-227x(97)89638-4. [DOI] [PubMed] [Google Scholar]
  4. Crowther R. A., Henderson R., Smith J. M. MRC image processing programs. J Struct Biol. 1996 Jan-Feb;116(1):9–16. doi: 10.1006/jsbi.1996.0003. [DOI] [PubMed] [Google Scholar]
  5. Darst S. A., Ahlers M., Meller P. H., Kubalek E. W., Blankenburg R., Ribi H. O., Ringsdorf H., Kornberg R. D. Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules. Biophys J. 1991 Feb;59(2):387–396. doi: 10.1016/S0006-3495(91)82232-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Frank J., Chiu W., Degn L. The characterization of structural variations within a crystal field. Ultramicroscopy. 1988;26(4):345–360. doi: 10.1016/0304-3991(88)90234-3. [DOI] [PubMed] [Google Scholar]
  7. Frey W., Schief W. R., Jr, Pack D. W., Chen C. T., Chilkoti A., Stayton P., Vogel V., Arnold F. H. Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines. Proc Natl Acad Sci U S A. 1996 May 14;93(10):4937–4941. doi: 10.1073/pnas.93.10.4937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fukami A., Adachi K. A new method of preparation of a self-perforated micro plastic grid and its application. J Electron Microsc (Tokyo) 1965;14(2):112–118. [PubMed] [Google Scholar]
  9. 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]
  10. Hemming S. A., Bochkarev A., Darst S. A., Kornberg R. D., Ala P., Yang D. S., Edwards A. M. The mechanism of protein crystal growth from lipid layers. J Mol Biol. 1995 Feb 17;246(2):308–316. doi: 10.1006/jmbi.1994.0086. [DOI] [PubMed] [Google Scholar]
  11. Hendrickson W. A., Pähler A., Smith J. L., Satow Y., Merritt E. A., Phizackerley R. P. Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation. Proc Natl Acad Sci U S A. 1989 Apr;86(7):2190–2194. doi: 10.1073/pnas.86.7.2190. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kubalek E. W., Kornberg R. D., Darst S. A. Improved transfer of two-dimensional crystals from the air/water interface to specimen support grids for high-resolution analysis by electron microscopy. Ultramicroscopy. 1991 Jun;35(3-4):295–304. doi: 10.1016/0304-3991(91)90082-h. [DOI] [PubMed] [Google Scholar]
  13. Lösche M., Piepenstock M., Diederich A., Grünewald T., Kjaer K., Vaknin D. Influence of surface chemistry on the structural organization of monomolecular protein layers adsorbed to functionalized aqueous interfaces. Biophys J. 1993 Nov;65(5):2160–2177. doi: 10.1016/S0006-3495(93)81269-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pähler A., Hendrickson W. A., Kolks M. A., Argaraña C. E., Cantor C. R. Characterization and crystallization of core streptavidin. J Biol Chem. 1987 Oct 15;262(29):13933–13937. [PubMed] [Google Scholar]
  15. Schmid C., Schläpfer I., Gosteli-Peter M. A., Froesch E. R., Zapf J. Expression, effects, and fate of IGFBP-5 are different in normal and malignant osteoblastic cells. Prog Growth Factor Res. 1995;6(2-4):167–173. doi: 10.1016/0955-2235(95)00037-2. [DOI] [PubMed] [Google Scholar]
  16. Schmid M. F., Dargahi R., Tam M. W. SPECTRA: a system for processing electron images of crystals. Ultramicroscopy. 1993 Mar;48(3):251–264. doi: 10.1016/0304-3991(93)90099-j. [DOI] [PubMed] [Google Scholar]
  17. Schmidt A., Spinke J., Bayerl T., Sackmann E., Knoll W. Streptavidin binding to biotinylated lipid layers on solid supports. A neutron reflection and surface plasmon optical study. Biophys J. 1992 Nov;63(5):1385–1392. doi: 10.1016/S0006-3495(92)81715-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Uzgiris E. E., Kornberg R. D. Two-dimensional crystallization technique for imaging macromolecules, with application to antigen--antibody--complement complexes. Nature. 1983 Jan 13;301(5896):125–129. doi: 10.1038/301125a0. [DOI] [PubMed] [Google Scholar]
  19. Veggeland T., Fagerheim K. U., Ritland T., Smørdal K., Arvik K. Vet pasienter nok om sine medisiner? En spørreundersøkelse foretatt ved fem norske sykehus blant pasienter utskrevet med hjertemedisin. Tidsskr Nor Laegeforen. 1993 Oct 10;113(24):3013–3016. [PubMed] [Google Scholar]
  20. Weber P. C., Ohlendorf D. H., Wendoloski J. J., Salemme F. R. Structural origins of high-affinity biotin binding to streptavidin. Science. 1989 Jan 6;243(4887):85–88. doi: 10.1126/science.2911722. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES