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Crystallization and preliminary X-ray diffraction analysis of the complex of human placental 17β-hydroxysteroid dehydrogenase with NADP+

  • D. W. Zhu
  • , X. Lee
  • , R. Breton
  • , D. Ghosh
  • , W. Pangborn
  • , W. L. Duax
  • , S. X. Lin
  • Université Laval
  • Cleveland Clinic Foundation
  • Hauptman-Woodward Medical Research Institute, Inc.

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

Single crystals of human placental 17β-hydroxysteroid dehydrogenase: an enzyme that plays an important role in the interconversion of estrogens, were obtained as the NADP+ complex. These are the first crystals suitable for complete X-ray structure analysis ever reported for a steroid-converting enzyme from a human source. The crystals were grown by vapor diffusion at pH 7.5 with polyethyleneglycol (4000) as the precipitating agent. They have a monoclinic space group C2 and unit cell parameters are a = 123.03 Å, b = 45.03 Å, c = 61.29 Å, and β = 99.1°. A complete set of diffraction data to 2.9 Å has been collected on native crystals.

Original languageEnglish
Pages (from-to)242-244
Number of pages3
JournalJournal of Molecular Biology
Volume234
Issue number1
DOIs
StatePublished - Nov 5 1993

Keywords

  • 17β-hydroxysteroid dehydrogenase
  • Crystallization
  • Steroid converting enzyme
  • X-ray diffraction

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