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Peer-reviewedCC BY 4.0Acta crystallographica Section F : Structural biology communications [2014-...]

Serendipitous crystal structure of mJuniper, a rationally designed cyan fluorescent protein

Abstract

mJuniper is a recently developed monomeric cyan fluorescent protein (CFP) optimized for bacterial imaging, distinguished by the fastest maturation kinetics recorded for a CFP. mJuniper shows significant promise for time-lapse microscopy, but was used here to improve the solubility of a target protein. Here, we report the high-resolution X-ray structure of mJuniper, obtained serendipitously during an attempted structural characterization of CagG, an essential component of the Helicobacter pylori Cag type IV secretion system. The structure reveals a classical β-barrel scaffold, as well as a chromophore with two rotameric states, resulting from specific radiation damage occurring in its vicinity.

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BibTeX
@article{aydin2026serendipitous,
  title = {{Serendipitous crystal structure of mJuniper, a rationally designed cyan fluorescent protein}},
  author = {Alpay Aydin and Nathan Fraikin and Priscillia Lagoutte and Christian Lesterlin and Laurent Terradot},
  journal = {Acta crystallographica Section F : Structural biology communications [2014-...]},
  year = {2026},
  month = sep,
  doi = {10.1107/s2053230x26009052},
  url = {https://hal.science/hal-05767043v1},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Serendipitous crystal structure of mJuniper, a rationally designed cyan fluorescent protein
AU  - Alpay Aydin
AU  - Nathan Fraikin
AU  - Priscillia Lagoutte
AU  - Christian Lesterlin
AU  - Laurent Terradot
PY  - 2026
DA  - 2026/09/17
JO  - Acta crystallographica Section F : Structural biology communications [2014-...]
DO  - 10.1107/s2053230x26009052
UR  - https://hal.science/hal-05767043v1
AB  - mJuniper is a recently developed monomeric cyan fluorescent protein (CFP) optimized for bacterial imaging, distinguished by the fastest maturation kinetics recorded for a CFP. mJuniper shows significant promise for time-lapse microscopy, but was used here to improve the solubility of a target protein. Here, we report the high-resolution X-ray structure of mJuniper, obtained serendipitously during an attempted structural characterization of CagG, an essential component of the Helicobacter pylori Cag type IV secretion system. The structure reveals a classical β-barrel scaffold, as well as a chromophore with two rotameric states, resulting from specific radiation damage occurring in its vicinity.
SN  - 2053-230X
ER  -