Crystallization and preliminary X-ray diffraction analysis of the diterpene cyclooctatin synthase (CYC) fromStreptomycessp. LZ35

Abstract

Terpenoids are a large and highly diverse group of natural products, with the most chemically diverse pool of structures. Terpene synthase is the key enzyme in the process of terpenoid synthesis. In this paper, the first diterpene synthase (CYC) of bacterial origin was successfully crystallized. Native and SeMetderivative crystals diffracted to 1.75 and 2.6 Å resolution, respectively. The native crystal belonged to space group P2 1 2 1 2 1 , with unit-cell parameters a = 59.10, b = 101.73, c = 108.93 Å , and contained two molecules per asymmetric unit. The SeMet-derivative crystal belonged to space group P2 1 , with unit-cell parameters a = 58.64, b = 109.47, c = 58.73 Å , = 119.35 , and had two molecules per asymmetric unit.