Work

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

Year: 2026

Type: article

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.

Source: Acta Crystallographica Section F Structural Biology Communications

DOI: 10.1107/s2053230x26009052

Authors: Alpay Aydin, Nathan Fraikin, Priscillia Lagoutte, Christian Lesterlin, Laurent Terradot

Institutions: Centre National de la Recherche Scientifique, Université de Lyon, Microbiologie moléculaire et biochimie structurale

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: European Synchrotron Radiation Facility, Ligue Contre le Cancer, Centre National de la Recherche Scientifique, Institut National de Physique Nucléaire et de Physique des Particules

Awards: G196419191, G3008589337, G6649312515, G8778376598