Crystallization and preliminary X-ray diffraction results of snowdrop (Galanthus nivalis) lectin.
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چکیده
منابع مشابه
Biosynthesis of the Snowdrop (Galanthus nivalis) Lectin in Ripening Ovaries.
The biosynthesis and processing of the Galanthus nivalis agglutinin were studied in vivo in ripening snowdrop ovaries. Using labeling and pulse chase labeling experiments it could be demonstrated that the snowdrop lectin is synthesized as a precursor of relative molecular weight (M(r)) 15,000 which is posttranslationally converted into the authentic lectin polypeptide of M(r) 13,000 with a half...
متن کاملBiosynthesis, primary structure and molecular cloning of snowdrop (Galanthus nivalis L.) lectin.
Poly(A)-rich RNA isolated from ripening ovaries of snowdrop (Galanthus nivalis L.) yielded a single 17-kDa lectin polypeptide upon translation in a wheat-germ cell-free system. This lectin was purified by affinity chromatography. Translation of the same RNA in Xenopus leavis oocytes revealed a lectin polypeptide which was about 2 kDa smaller than the in vitro synthesized precursor, suggesting t...
متن کاملCrystallization and preliminary X-ray diffraction
The amyloidogenic Leu55Pro variant of transthyretin has been expressed, purified and crystallized in space group C2. The cell constants are a--149.99, b = 78.74, c = 98.95A, = 100.5 ° and the crystals diffract to 2.7,~ resolution. There are eight monomers in the asymmetric unit giving a V M = 2.6,~,3 Da -w and 53% solvent content. In the wild-type protein, the crystals are orthorhombic with two...
متن کاملCrystallization and preliminary X-ray diffraction analysis of a lectin from Canavalia maritima seeds.
A lectin from Canavalia maritima seeds (ConM) was purified and submitted to crystallization experiments. The best crystals were obtained using the vapour-diffusion method at a constant temperature of 293 K and grew in 7 d. A complete structural data set was collected to 2.1 A resolution using a synchrotron-radiation source. The ConM crystal belongs to the orthorhombic space group P2(1)2(1)2, wi...
متن کاملCrystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia gladiata seeds.
The seed lectin from Canavalia gladiata was purified and crystallized. Orthorhombic crystals belonging to space group C222(1) grew within three weeks at 293 K using the hanging-drop vapour-diffusion method. Using synchrotron X-ray radiation, a complete structural data set was collected at 2.3 A resolution. The preliminary crystal structure of the lectin, determined by molecular replacement, had...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)40068-9