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Crystallization and preliminary X-ray diffraction studies of human RANTES

J P Shaw1, G Kryger, A Cleasby

  • 1Rosentiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.

Journal of Molecular Biology
|September 30, 1994
PubMed
Summary

Researchers crystallized the protein RANTES (Regulated on Activation, Normal T-cell Expressed and Secreted), a key immune cell signaling molecule. These crystals diffract X-rays to 1.8 A, enabling detailed structural analysis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • RANTES (Regulated on Activation, Normal T-cell Expressed and Secreted) is an 8 kDa chemotactic cytokine.
  • It acts as a potent chemoattractant and activator for various leukocytes.

Purpose of the Study:

  • To obtain high-quality crystals of the RANTES protein for structural determination.
  • To characterize the crystallographic properties of RANTES crystals.

Main Methods:

  • Crystallization was performed using a buffer containing sodium acetate, magnesium acetate, PEG 4000, and glycerol.
  • X-ray diffraction data were collected using a rotating anode X-ray source.

Main Results:

  • Thick rod-shaped crystals of RANTES were successfully grown.

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  • The crystals diffracted X-rays to a resolution of at least 1.8 A.
  • Crystallographic data revealed space group p2(1)2(1)2(1) with specific unit cell dimensions (a=95.14 A, b=57.58 A, c=24.01 A).
  • The asymmetric unit contains two RANTES monomer molecules.

    • Conclusions:

    • The study successfully established conditions for crystallizing RANTES.
    • The obtained crystals are suitable for high-resolution X-ray crystallography, paving the way for detailed structural studies of RANTES.