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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 1(67), p. 101-103, 2010

DOI: 10.1107/s1744309110046944

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Crystallization and preliminary X-ray analysis of isopentenyl diphosphate isomerase fromMethanocaldococcus jannaschii

Journal article published in 2010 by Takeshi Hoshino, Eriko Nango, Seiki Baba, Tadashi Eguchi, Takashi Kumasaka ORCID
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

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 (VM) of 3.0 Å3 Da(-1) and a solvent constant of 59.0% by volume.