Crystallization of retinol dehydratase from Spodoptera frugiperda: improvement of crystal quality by modification by ethylmercurythiosalicylate.

Retinol dehydratase is a sulfotransferase which is presumed to catalyze the dehydration of its substrate via a transient retinyl sulfate intermediate. Crystals (space group P2(1), unit-cell parameters a = 82.05, b = 66.61, c = 84.90 A, beta = 111.29 degrees ) are significantly improved by covalent modification of the protein with ethylmercury.
AuthorsS Pakhomova, J G Luz, M Kobayashi, D Mellman, J Buck, M E Newcomer
JournalActa crystallographica. Section D, Biological crystallography (Acta Crystallogr D Biol Crystallogr) Vol. 56 Issue Pt 12 Pg. 1641-3 (Dec 2000) ISSN: 0907-4449 [Print] DENMARK
PMID11092933 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Benzoates
  • Ethylmercury Compounds
  • ethylmercury thiosalicylate
  • Thimerosal
  • Hydro-Lyases
  • retinol dehydratase
  • Animals
  • Benzoates (chemistry)
  • Crystallization
  • Ethylmercury Compounds (chemistry)
  • Hydro-Lyases (chemistry)
  • Models, Molecular
  • Protein Conformation
  • Spodoptera (enzymology)
  • Thimerosal
  • X-Ray Diffraction

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research network!

Choose Username:
Verify Password: