Crystallization and preliminary X-ray diffraction analysis of cyclolavandulyl diphosphate synthase, a new member of the cis-isoprenyl diphosphate synthase superfamily

Cyclolavandulyl diphosphate synthase (CLDS; estimated molecular weight 23.1 kDa) from the soil bacterium Streptomyces sp. CL190 is an enzyme that catalyzes both the condensation of two molecules of C5 dimethylallyl diphosphate (DMAPP) and the subsequent cyclization. CLDS was crystallized in the absence and the presence of the substrate DMAPP. Diffraction data were collected at a synchrotron source and the crystals diffracted to 2.00 and 1.73 Å resolution, respectively. The crystal obtained in the absence of DMAPP belonged to space group P212121, with unit-cell parameters a = 39.0, b = 87.5, c = 113.6 Å. The crystal obtained in the presence of DMAPP belonged to space group P1, with unit-cell parameters a = 46.9, b = 61.7, c = 82.2 Å, α = 74.0, β = 84.5, γ = 86.0°.

Source: Acta Crystallographica Section F - September 25, 2014 Category: Biochemistry Authors: Tomita, T.Ozaki, T.Matsuda, K.Nishiyama, M.Kuzuyama, T. Tags: condensing enzyme cyclase cyclolavandulyl diphosphate synthase Streptomyces sp. CL190 terpene crystallization communications Source Type: research