Data of crystal structure of the monomeric red fluorescent protein DsRed

Abstract

The monomeric red fluorescent protein DsRed (mDsRed) is an optical probe widely used in multicolor applications in flow cytometry and fluorescence microscopy. Although the crystal structure of monomeric DsRed has been determined, its molecular dynamics have not been fully elucidated. To better understand its molecular flexibility, the crystal structure of mDsRed was recently determined, and its structure and temperature factors were analyzed. Solvent-accessible hole connected with the mDsRed chromophore was observed on the mDsRed surface structure. Electron density map analysis showed the tyrosine-ring group of the mDsRed chromophore in a cis-conformation, exhibiting flexibility with a nonplanar configuration between the tyrosine and imidazoline rings of the chromophore. Temperature factor analysis indicated that the top and bottom of the β-barrel are relatively flexible. These structural findings extended our understanding of the molecular flexibility of mDsRed. The detailed data collection and structure determination reported in this study can be used for future structural analyses.

Keywords

• Substrate binding protein
• Single domain
• Structural flexibility
• X-ray diffraction data
• Crystal structure