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Related Experiment Videos

Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data.

Wayne W Chan1, Steven L Roderick, David E Cohen

  • 1Department of Medicine, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.

Biochimica Et Biophysica Acta
|May 2, 2002
PubMed
Summary

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Researchers purified and crystallized human phosphatidylcholine transfer protein (PC-TP) and a selenomethionyl variant. Their biochemical properties were identical, enabling crystallization for X-ray diffraction studies.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Crystallography

Background:

  • Phosphatidylcholine transfer protein (PC-TP) plays a role in lipid metabolism.
  • Understanding PC-TP structure is crucial for elucidating its function.

Purpose of the Study:

  • To express, purify, and crystallize recombinant human PC-TP.
  • To obtain high-resolution structural data of PC-TP.

Main Methods:

  • Recombinant expression and purification of native and selenomethionyl PC-TP.
  • Crystallization of PC-TP bound to dilinoleoyl phosphatidylcholine.
  • X-ray diffraction analysis of protein crystals.

Main Results:

  • Native and selenomethionyl PC-TP were successfully expressed and purified.

Related Experiment Videos

  • Biochemical properties of both protein forms were indistinguishable.
  • Both protein forms crystallized in two distinct space groups, diffracting X-rays to 2.4 Å resolution.

    • Conclusions:

    • The methods used are suitable for obtaining structural information on PC-TP.
    • The indistinguishable properties of native and selenomethionyl PC-TP facilitate structural studies.
    • High-resolution structural data of PC-TP can be obtained via X-ray crystallography.