Purification, crystallization and initial X-ray analysis of the C-1 subunit of the astaxanthin protein, V-600 of the chondrophore Velella velella

Citation
Ne. Chayen et al., Purification, crystallization and initial X-ray analysis of the C-1 subunit of the astaxanthin protein, V-600 of the chondrophore Velella velella, ACT CRYST D, 55, 1999, pp. 266-268
Citations number
18
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
55
Year of publication
1999
Part
1
Pages
266 - 268
Database
ISI
SICI code
0907-4449(199901)55:<266:PCAIXA>2.0.ZU;2-F
Abstract
The subunit C-1 of the carotenoid-binding protein, V-600, of the chondropho re Velella velella has been purified and crystallized. The crystals, which were grown by the vapour-diffusion method from ammonium sulfate as the majo r precipitant, diffract beyond 3 Angstrom and show little radiation damage over long periods (greater than 100 h) on a Cu K alpha rotating-anode X-ray source. The space group of the crystals is P2(1)2(1)2(1) with cell dimensi ons a = 42.0, b = 80.9, c = 110.6 Angstrom.