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Bovine P2 myelin basic protein crystallizes in three different forms.

J Sedzik1, T Bergfors, T A Jones

  • 1Department of Molecular Biology, University of Uppsala, Sweden.

Journal of Neurochemistry
|June 1, 1988
PubMed
Summary
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Researchers crystallized the P2 protein, a myelin membrane component, for high-resolution study. The resulting crystals, grown with PEG 4000, diffract X-rays to 2.7 angstroms.

Area of Science:

  • Structural biology
  • Neuroscience
  • Biochemistry

Background:

  • P2 protein is a minor but significant component of the myelin sheath.
  • Understanding myelin structure is crucial for neurological research.

Purpose of the Study:

  • To obtain high-resolution structural data of the P2 protein.
  • To facilitate crystallographic analysis of myelin components.

Main Methods:

  • Crystallization of P2 protein using various precipitants.
  • Screening of crystal morphologies, including ammonium sulfate and polyethylene glycol (PEG).
  • X-ray diffraction analysis of PEG 4000-grown crystals.

Main Results:

  • Three distinct crystal morphologies were obtained.

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  • The most suitable crystals were grown using PEG 4000.
  • These crystals belong to space group P2(1)2(1)2(1) with unit cell dimensions a = 91.3 A, b = 99.8 A, c = 56.0 A.
  • The crystal structure can be resolved to 2.7 angstroms.
  • Up to four molecules per asymmetric unit were identified.

    • Conclusions:

    • High-quality crystals of P2 protein suitable for detailed structural studies have been produced.
    • The crystallographic data obtained will enable precise determination of the P2 protein's three-dimensional structure.
    • This structural information is vital for understanding myelin structure and function.