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

被引:5
作者
Chayen, NE
Boggon, TJ
Raftery, J
Helliwell, JR
Zagalsky, PF
机构
[1] Univ London Imperial Coll Sci Technol & Med, Blackett Lab, Biophys Sect, London SW7 2BZ, England
[2] Univ London Royal Holloway & Bedford New Coll, Dept Biochem, Egham TW20 0EX, Surrey, England
[3] Univ Manchester, Dept Chem, Struct Chem Sect, Manchester M13 9PL, Lancs, England
[4] Univ London Royal Holloway & Bedford New Coll, Dept Biochem, Egham TW20 0EX, Surrey, England
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷
基金
英国惠康基金;
关键词
D O I
10.1107/S0907444998006908
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The subunit C-1 of the carotenoid-binding protein, V-600, 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 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 dimensions a = 42.0, b = 80.9, c = 110.6 Angstrom.
引用
收藏
页码:266 / 268
页数:3
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