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Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Aug2013, Vol. 69 Issue 8, p937-941. 5p. - Publication Year :
- 2013
-
Abstract
- Glycinin is one of the most abundant storage-protein molecules in soybean seeds and is composed of five subunits (A1aB1b, A1bB2, A2B1a, A3B4 and A5A4B3). A1bB2 was purified from a mutant soybean cultivar containing glycinin composed of only A5A4B3 and A1bB2. At 281 K the protein formed hexagonal, rectangular and rod-shaped crystals in the first [0.1 M imidazole pH 8.0, 0.2 M MgCl2, 35%( v/ v) MPD], second [0.1 M sodium citrate pH 5.6, 0.2 M ammonium acetate, 30%( v/ v) MPD] and third (0.1 M phosphate-citrate pH 4.2, 2.0 M ammonium sulfate) crystallization conditions, respectively. X-ray diffraction data were collected to resolutions of 1.85, 1.85 and 2.5 Å from crystals of the three different shapes. The crystals belonged to space groups P6322, P21 and P1, with unit-cell parameters a = b = 143.60, c = 84.54 Å, a = 114.54, b = 105.82, c = 116.67 Å, β = 94.99° and a = 94.45, b = 94.96, c = 100.66 Å, α = 107.02, β = 108.44, γ = 110.71°, respectively. One, six and six subunits of A1bB2 were estimated to be present in the respective asymmetric units. The three-dimensional structure of the A1bB2 hexamer is currently being determined. [ABSTRACT FROM AUTHOR]
- Subjects :
- *GLYCININ
*SEEDS
*SOYBEAN
*CRYSTALLOGRAPHIC shear
*CRYSTALLIZATION
*AMMONIUM sulfate
Subjects
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 69
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 89468482
- Full Text :
- https://doi.org/10.1107/S1744309113019684