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

Cyclolavandulyl diphosphate synthase (CLDS; estimated molecular weight 23.1 kDa) from the soil bacteriumStreptomycessp. CL190 is an enzyme that catalyzes both the condensation of two molecules of C5dimethylallyl 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 groupP212121, with unit-cell parametersa= 39.0,b= 87.5,c= 113.6 Å. The crystal obtained in the presence of DMAPP belonged to space groupP1, with unit-cell parametersa= 46.9,b= 61.7,c= 82.2 Å, α = 74.0, β = 84.5, γ = 86.0°.