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Comparison List

StayGold-E138D

a.k.a. mStayGold

StayGold-E138D is a basic (constitutively fluorescent) green fluorescent protein published in 2023, derived from Cytaeis uchidae. It is reported to be a very rapidly-maturing monomer with low acid sensitivity.
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Oligomerization Organism Molecular Weight Cofactor
Monomer Cytaeis uchidae 24.6 kDa -

FPbase ID: Q8WTP

Attributes

Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
497 504 145,000 0.87 126.15 4.6 14.0  

Photostability

t1/2 (s) Power Light Mode In Cell Fusion ˚C Reference
1260.0 7.4 (W/cm2) Laser Spinning Disc Confocal HeLa (fixed) TPM2 25.0 Ivorra-Molla et al. (2023)
74.0 29.0 (W/cm2) Laser Other 25.0 Ivorra-Molla et al. (2023)

StayGold-E138D Sequence

StayGold-E138D was derived from StayGold with the following mutations: E138D

MASTPFKFQLKGTINGKSFTVEGEGEGNSHEGSHKGKYVCTSGKLPMSWAALGTSFGYGMKYYTKYPSGLKNWFHEVMPEGFTYDRHIQYKGDGSIHAKHQHFMKNGTYHNIVEFTGQDFKENSPVLTGDMNVSLPNDVQHIPRDDGVECPVTLLYPLLSDKSKCVEAHQNTICKPLHNQPAPDVPYHWIRKQYTQSKDDTEERDHICQSETLEAHL

Excerpts

StayGold is an exceptionally bright and stable fluorescent protein that is highly resistant to photobleaching. Despite favourable fluorescence properties, use of StayGold as a fluorescent tag is limited because it forms a natural dimer. Here we describe the 1.6 Å structure of StayGold and generate a new derivative (mStayGold) that retains the brightness and photostability of the original protein while being fully monomeric.

Ivorra-Molla et al. (2023)

to establish monomerization in vivo, we performed the organized smooth endoplasmic reticulum (OSER) assay for StayGold and mStayGold E138D alongside dTomato (an established dimer) and mTurquoise (a known monomer; Supplementary Fig. 14). The data show that mStayGold E138D is monomeric, with an OSER score comparable to that of the mTurquoise control, while the original StayGold is a weak dimer, with an OSER score that is lower than mStayGold but higher than dTomato. The apparent fragility of the StayGold dimer in the OSER assay is consistent with our observation that the interface can easily be broken with single amino acid substitutions.

Ivorra-Molla et al. (2023)

Primary Reference

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