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The antibiotic bacillaene is biosynthesized in Bacillus subtilis by a hybrid type 1 modular polyketide synthase/nonribosomal peptide synthetase of the transacyltransferase (trans-AT) class. Within this system, the essential acyl-group loading activity is provided by the action of three free-standing trans-acting acyltransferases. Here, the recombinant expression, purification and crystallization of the bacillaene synthase trans-acting acyltransferase PksC are reported. A diffraction data set has been collected from a single PksC crystal to 1.44 A ° resolution and the crystal was found to belong to the orthorhombic space group P212121.
|Translated title of the contribution||Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC|
|Pages (from-to)||464 - 466|
|Number of pages||3|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - Apr 2011|