Journal
NATURE METHODS
Volume 12, Issue 8, Pages 763-U106Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.3447
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Funding
- Program for Breakthrough Biomedical Research
- US National Institute of Health (NIH) [GM030637, GM084040, GM096164]
- Howard Hughes Medical Institute
- NIH [GM054616]
- US National Science Foundation [DMR-1120901]
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [T32HD007470] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM084040, R01GM054616, R35GM118167, R37GM054616, R01GM030637, R01GM096164] Funding Source: NIH RePORTER
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Infrared fluorescent proteins (IFPs) provide an additional color to GFP and its homologs in protein labeling. Drawing on structural analysis of the dimer interface, we identified a bacteriophytochrome in the sequence database that is monomeric in truncated form and engineered it into a naturally monomeric IFP (mIFP). We demonstrate that mIFP correctly labels proteins in live cells, Drosophila and zebrafish. It should be useful in molecular, cell and developmental biology.
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