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  1. Home
  3. Data Of Crystal Structure Of The Large Stokes Shift Fluorescent Protein Tkeima.
  1. Home
  3. Data Of Crystal Structure Of The Large Stokes Shift Fluorescent Protein Tkeima.

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Data of crystal structure of the large Stokes shift fluorescent protein tKeima.

Ki Hyun Nam1, Yongbin Xu2,3

  • 1College of General Education, Kookmin University, Seoul 02707, Republic of Korea.

Data in Brief
|October 1, 2024

View abstract on PubMed

Summary
This summary is machine-generated.

Researchers detailed experimental procedures for tKeima, a large Stokes shift (LSS) fluorescent protein (FP). This work aids understanding of tetrameric FP structure and engineering efforts for monomeric fluorescent proteins.

Keywords:
Crystal structureFluorescent proteinLarge stroke shiftX-ray diffractiontKeima

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Large Stokes shift (LSS) fluorescent proteins (FPs) are crucial for advanced imaging techniques like dual-color fluorescence cross-correlation spectroscopy and multicolor imaging.
  • tKeima, a tetrameric LSS FP from *Montipora* sp., is a key protein for studying FP oligomerization.
  • Understanding the tetrameric interface of tKeima is vital for engineering monomeric FPs, which are valuable tools in molecular and cell biology.

Purpose of the Study:

  • To report detailed experimental procedures for tKeima, facilitating future high-resolution structural studies.
  • To provide a foundation for analyzing the tetrameric interface of tKeima.
  • To offer insights into the protein engineering of oligomeric FPs, particularly for developing monomeric variants.

Main Methods:

  • Spontaneous crystal growth of tKeima.
  • X-ray diffraction data collection.
  • Structure determination of tKeima.

Main Results:

  • Detailed experimental protocols for tKeima crystallization and X-ray diffraction were established.
  • The study lays the groundwork for obtaining high-resolution structural data of tKeima.
  • This procedural information is essential for future structural and engineering applications.

Conclusions:

  • The reported procedures enable future high-resolution structure determination of tKeima.
  • Structural insights will enhance understanding of tKeima's molecular function and tetrameric FP engineering.
  • This work supports the development of novel monomeric fluorescent proteins for biological applications.