The only way to obtain a clear picture of the structure of these proteins is the generation of 2-dimensional or 3-dimensional crystals or the structural analysis of purified protein by NMR. For most membrane proteins, however, already the first steps towards any of these techniques are hindered by the low expression levels of these proteins, by their extreme hydrophobicity and the concomitant difficulties during purification.The attachment of hydrophilic tags to such proteins has become an important tool to overcome at least part of these problems [9 12]. The present paper describes the advantages of a bacterial biotin acceptor domain for the one-step purification of the recombinant P major sucrose carrier PmSUC2 [13] from transgenic yeast.
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