Brief Communication abstract
Nature Methods 6, 355 - 358 (2009)
Published online: 12 April 2009 | doi:10.1038/nmeth.1319
Photoconversion in orange and red fluorescent proteins
Gert-Jan Kremers1, Kristin L Hazelwood2, Christopher S Murphy2, Michael W Davidson2 & David W Piston1
We found that photoconversion is fairly common among orange and red fluorescent proteins, as in a screen of 12 proteins, 8 exhibited photoconversion. Specifically, three red fluorescent proteins could be switched to a green state, and two orange variants could be photoconverted to a far-red state. The orange proteins are ideal for dual-probe highlighter applications, and they exhibited the most red-shifted excitation of all fluorescent proteins described to date.
- Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee, USA.
- National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, Florida, USA.
Correspondence to: David W Piston1 e-mail: dave.piston@vanderbilt.edu
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