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Large scale purification and structural properties of yeast aspartyl-tRNA synthetase
Authors:B Lorber  D Kern  A Dietrich  J Gangloff  J P Ebel  R Giegé
Institution:Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., 15, rue René Descartes, F - 67084 Strasbourg Cedex, France
Abstract:A large scale purification procedure of baker's yeast aspartyl-tRNA synthetase is described which yields more than 200 mg pure protein starting from 30 Kg of wet commercial cells. The synthetase is an alpha 2 dimer of Mr = 125,000 +/- 5,000 which can be crystallized (J. Mol. Biol. 138, 1980, 129-135). The enzyme has an elongated shape with a Stokes radius of 50 A and a frictional ratio of 1.5. The synthetase has a tendency to aggregate but methods are described where this effect is overcome.
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