Crystallization and preliminary X‐ray analysis of isopentenyl diphosphate isomerase from Methanocaldococcus jannaschii
Type 2 isopentenyl diphosphate isomerase (IDI‐2) is a flavoprotein. Recently, flavin has been proposed to play a role as a general acid–base catalyst with no redox role during the enzyme reaction. To clarify the detailed enzyme reaction mechanism of IDI‐2 and the unusual role of flavin, structural analysis of IDI‐2 from Methanocaldococcus jannaschii (MjIDI) was performed. Recombinant MjIDI was crystallized at 293 K using calcium acetate as a precipitant. The diffraction of the crystal extended to 2.08 Å resolution at 100 K. The crystal belonged to the tetragonal space group I422, with unit‐cell parameters a = 126.46, c = 120.03 Å. The presence of one monomer per asymmetric unit gives a crystal volume per protein weight (V M) of 3.0 Å3 Da−1 and a solvent constant of 59.0% by volume.
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