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Crystallographic data for soybean hydrophobic protein.

M S Lehmann1, E Pebay-Peyroula, C Cohen-Addad

  • 1Institut Laue-Langevin, Grenoble, France.

Journal of Molecular Biology
|November 5, 1989
PubMed
Summary

Soybean hydrophobic protein, a membrane protein, was crystallized for structural analysis. Its exact function remains unknown, but its properties suggest potential roles in cellular processes.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Plant Science

Background:

  • Soybean hydrophobic protein is part of a protein family including storage and phospholipid-binding proteins.
  • Its precise function is currently unknown.
  • Its hydrophobic nature is characteristic of membrane proteins of comparable size.

Purpose of the Study:

  • To characterize the soybean hydrophobic protein.
  • To determine its suitability for X-ray structural studies.

Main Methods:

  • Crystallization of the soybean hydrophobic protein.
  • X-ray diffraction analysis.

Main Results:

  • The protein has a molecular weight of 8.3 kDa.

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  • It crystallizes in space group P2(1)2(1)2(1) with unit cell dimensions a = 52.01 Å, b = 43.50 Å, c = 28.80 Å.
  • The crystals diffract X-rays to 1.8 Å resolution.

    • Conclusions:

    • The determined crystal properties indicate suitability for detailed X-ray structural studies.
    • Structural elucidation could provide insights into the protein's function.