Crystallization of barley malt alpha-amylases and preliminary x-ray diffraction studies of the high pI isozyme, alpha-amylase 2.
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چکیده
منابع مشابه
Crystallization and preliminary X-ray diffraction studies of soybean agglutinin.
Soybean agglutinin crystallizes in the monoclinic space group C2 with unit cell dimensions a = 118.6 A, b = 88.9 A, c = 165.9 A, beta = 103.0 degrees and one tetramer of 120,000 Mr per asymmetric unit. The crystals are suitable for high-resolution work.
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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...
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Deletion analysis has previously shown that the major gibberellic acid (GA)- and abscisic acid (ABA)-responsive elements in the promoter of a high-pI alpha-amylase gene of barley are located downstream of -174 (Jacobsen and Close, 1991). We have used transient expression assays in barley aleurone protoplasts to identify sequences between -174 and +53 that confer GA and ABA responsiveness on exp...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)76480-1