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

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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 sou...

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ژورنال

عنوان ژورنال: Acta Crystallographica Section F Structural Biology Communications

سال: 2014

ISSN: 2053-230X

DOI: 10.1107/s2053230x14018883