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Published August 2014 | Accepted Version
Journal Article Open

The structure of a far-red fluorescent protein, AQ143, shows evidence in support of reported red-shifting chromophore interactions


Engineering fluorescent proteins (FPs) to emit light at longer wavelengths is a significant focus in the development of the next generation of fluorescent biomarkers, as far-red light penetrates tissue with minimal absorption, allowing better imaging inside of biological hosts. Structure-guided design and directed evolution have led to the discovery of red FPs with significant bathochromic shifts to their emission. Here, we present the crystal structure of one of the most bathochromically shifted FPs reported to date, AQ143, a nine-point mutant of aeCP597, a chromoprotein from Actinia equina. The 2.19 Å resolution structure reveals several important chromophore interactions that contribute to the protein's far-red emission and shows dual occupancy of the green and red chromophores.

Additional Information

© 2014 The Protein Society. Received: Apr 04, 2014; Revised: May 28, 2014; Accepted: May 29, 2014. Published online 3 June 2014 proteinscience.org The authors are grateful for the use of beamline 12-2 at the Stanford Synchrotron Radiation Lightsource (SSRL) in Menlo Park, CA, operated by Stanford University and supported by the Department of Energy and the National Institutes of Health. They additionally are thankful to Jens Kaiser and Pavle Nikolovski at the California Institute of Technology for helpful discussions. Finally they thank the Gordon and Betty Moore Foundation, the Beckman Institute, and the Sanofi-Aventis Bioengineering Research Program for support of the Molecular Observatory at the California Institute of Technology.

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Accepted Version - Wannier_2014.pdf


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