Related Experiment Video
Updated: Sep 19, 2026

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect
Published on: March 19, 2019
Serendipitous crystal structure of mJuniper, a rationally designed cyan fluorescent protein
Alpay Aydin1, Nathan Fraikin1, Priscillia Lagoutte1
1Molecular Microbiology and Structural Biochemistry, UMR5086, Université de Lyon, CNRS, 69007 Lyon, France.
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.
More Related Videos
10:31Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
Published on: February 3, 2022
11:51Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
Published on: April 27, 2018