Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Click Me!

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 2 October 1987:
Vol. 238. no. 4823, pp. 36 - 41
DOI: 10.1126/science.3116667

Articles

Science, Vol 238, Issue 4823, 36-41
Copyright © 1987 by American Association for the Advancement of Science


articles

The use of a charge-coupled device for quantitative optical microscopy of biological structures

Y Hiraoka, JW Sedat, and DA Agard

Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.

The properties of a charge-coupled device (CCD) and its application to the high-resolution analysis of biological structures by optical microscopy are described. The CCD, with its high resolution, high sensitivity, wide dynamic range, photometric accuracy, and geometric stability, can provide data of such high quality that quantitative analysis on two- and three-dimensional microscopic images is possible. For example, the three-dimensional imaging properties of an epifluorescence microscope have been quantitatively determined with the CCD. This description of the imaging properties of the microscope, and the high-quality image data provided by the CCD, allow sophisticated computational image processing methods to be used that greatly improve the effective resolution obtainable for biological structures. Image processing techniques revealed fine substructures in Drosophila embryonic diploid chromosomes in two and three dimensions. The same approach can be extended to structures as small as yeast chromosomes or to other problems in structural cell biology.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Protein 4.2 is critical to CD47-membrane skeleton attachment in human red cells.
K. N. Dahl, R. Parthasarathy, C. M. Westhoff, D. M. Layton, and D. E. Discher (2004)
Blood 103, 1131-1136
   Abstract »    Full Text »    PDF »
Analysis of Integral Membrane Protein Contributions to the Deformability and Stability of the Human Erythrocyte Membrane.
H. M. Van Dort, D. W. Knowles, J. A. Chasis, G. Lee, N. Mohandas, and P. S. Low (2001)
J. Biol. Chem. 276, 46968-46974
   Abstract »    Full Text »    PDF »
High Tolerance and Delayed Elastic Response of Cultured Axons to Dynamic Stretch Injury.
D. H. Smith, J. A. Wolf, T. A. Lusardi, V. M.-Y. Lee, and D. F. Meaney (1999)
J. Neurosci. 19, 4263-4269
   Abstract »    Full Text »    PDF »
HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection.
M. A. Vodicka, D. M. Koepp, P. A. Silver, and M. Emerman (1998)
Genes & Dev. 12, 175-185
   Abstract »    Full Text »
Superresolution three-dimensional images of fluorescence in cells with minimal light exposure.
W. Carrington, R. Lynch, E. Moore, G Isenberg, K. Fogarty, and F. Fay (1995)
Science 268, 1483-1487
   Abstract »    PDF »
Mapping of adherens junction components using microscopic resonance energy transfer imaging.
Z Kam, T Volberg, and B Geiger (1995)
J. Cell Sci. 108, 1051-1062
   Abstract »    PDF »
Molecular maps of red cell deformation: hidden elasticity and in situ connectivity.
D. Discher, N Mohandas, and E. Evans (1994)
Science 266, 1032-1035
   Abstract »    PDF »
Causes of the liability insurance crisis.
S Harrington and R. Litan (1988)
Science 239, 737-741
   Abstract »    PDF »



ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)