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

Abstract
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
Topics
  • Animals
  • Benzoates (chemistry)
  • Crystallization
  • Ethylmercury Compounds (chemistry)
  • Hydro-Lyases (chemistry)
  • Models, Molecular
  • Protein Conformation
  • Spodoptera (enzymology)
  • Thimerosal
  • X-Ray Diffraction

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