Crystallization and preliminary X‐ray diffraction analysis of recombinant pentalenene synthase

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Abstract
Recombinant pentalenene synthase, a 42.5-kDa sesquiterpene cyclase originally isolated from Streptomyces UC5319 and cloned in Escherichia coli, has been crystallized in space group P63 with unit cell dimensions a = b = 183.5 Å and c = 56.5 Å. Hexagonal prismatic crystals, approximately 0.2 × 0.2 × 0.3 mm, diffract to approximately 2.9 Å resolution using monochromatic synchrotron radiation. From the universal (and achiral) building block, farnesyl pyrophosphate, pentalenene synthase catalyzes the formation of four stereocenters in the construction of the three fused five-membered rings of pentalenene; this novel sesquiterpene is a precursor to the pentalenolactone family of antibiotics.