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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 May 1;90(9):3811–3814. doi: 10.1073/pnas.90.9.3811

Atomic force microscopy of biochemically tagged DNA.

M N Murray 1, H G Hansma 1, M Bezanilla 1, T Sano 1, D F Ogletree 1, W Kolbe 1, C L Smith 1, C R Cantor 1, S Spengler 1, P K Hansma 1, et al.
PMCID: PMC46395  PMID: 8483898

Abstract

Small fragments of DNA of known length were made with the polymerase chain reaction. These fragments had biotin molecules covalently attached at their ends. They were subsequently labeled with a chimeric protein fusion between streptavidin and two immunoglobulin G-binding domains of staphylococcal protein A. This tetrameric species was expected to bind up to four DNA molecules via their attached biotin moieties. The DNA-protein complex was deposited on mica and imaged with an atomic force microscope. The images revealed the protein chimera at the expected location at the ends of the strands of DNA as well as the expected dimers, trimers, and tetramers of DNA bound to a single protein.

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Selected References

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