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Crystallization of prostatic binding protein

  • John S. Punzi
  • , Debashis Ghosh
  • , Charles M. Weeks
  • , Patrick Van Roey
  • , William L. Duax
  • Hauptman-Woodward Medical Research Institute, Inc.

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Prostatic binding protein is a dimeric glycoprotein capable of binding a variety of steroids. This protein is a major component of rat prostate cytosol making it possible to purify milligram quantities. Hexagonal crystals of X-ray diffraction quality have been grown from phosphate buffered ammonium sulfate solution by vapor diffusion methods. These crystals which are reasonably stable to X-rays, show diffraction to 6.3 Å and belong to space group P61 or P6122 or the enantiomorphs. The unit cell has dimensions a = 88.7(5) Å, c = 405(2) Å, contains 24 molecules and has a specific volume of 2.8 Å3/Dalton.

Original languageEnglish
Pages (from-to)365-370
Number of pages6
JournalJournal of Steroid Biochemistry
Volume31
Issue number4 PART 1
DOIs
StatePublished - Oct 1988

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