StayRose: a photostable StayGold derivative red-shifted by genetic code expansion was published in the Journal of Biological Chemistry last week by a team of scientists from the groups of Mohan Balasubramanian (WMS), Masanori Mishima (WMS), Allister Crow (SLS), Falk Schneider (WMS), Abhishek Kumar (Marine Biological Laboratory) and Lijiang Song (Warwick Chemistry), funded by a collaborative Wellcome Trust bioimaging grant.
This work was led by first author Dr Will Smith, who completed his PhD as part of the MRC DTP.
The work presents a new fluorescent protein named StayRose, which is the first red version of the photobleaching-resistant green protein StayGold. These photostable proteins can be tagged to proteins of interest for microscopy and overcome the previous issue of fluorescence loss during prolonged imaging. StayRose contains an unnatural amino acid, 3-aminotyrosine, which underpins its red colour. Tests showed that StayRose maintains the extreme photostability of StayGold. The work presents a StayRose crystal structure, the first of a 3-aminotyrosine-incorporating fluorescent protein, and demonstrates use of StayRose in bacteria and zebrafish embryos. 
Read the paper here.Link opens in a new window