Purification, crystallization and initial X-ray analysis of the C1 subunit of the astaxanthin protein, V600, of the chondrophore Velella velella

Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):266-8. doi: 10.1107/S0907444998006908. Epub 1999 Jan 1.

Abstract

The subunit C1 of the carotenoid-binding protein, V600, of the chondrophore Velella velella has been purified and crystallized. The crystals, which were grown by the vapour-diffusion method from ammonium sulfate as the major precipitant, diffract beyond 3 A and show little radiation damage over long periods (greater than 100 h) on a Cu Kalpha rotating-anode X-ray source. The space group of the crystals is P212121 with cell dimensions a = 42.0, b = 80.9, c = 110. 6 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Hydra / chemistry*
  • Protein Conformation
  • Xanthophylls
  • beta Carotene / analogs & derivatives*
  • beta Carotene / chemistry
  • beta Carotene / isolation & purification

Substances

  • Xanthophylls
  • beta Carotene
  • astaxanthine