Expression, purification, crystallization and preliminary X-ray studies of geranylgeranyl diphosphate synthase from Thermus thermophilus HB8

Authors: Nishio K.; Nodake Y.; Hamada K.; Suto K.; Nakagawa N.; Kuramitsu S.; Miura K.

Source: Acta Crystallographica Section D, Volume 60, Number 1, 1 January 2004 , pp. 178-180(3)

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Abstract:

Geranylgeranyl diphosphate (GGPP) synthase from Thermus thermophilus HB8 was expressed in Escherichia coli, purified to homogeneity and crystallized both as the recombinant native protein and its selenomethionine (SeMet) derivative. Well diffracting crystals of these proteins were obtained belonging to the tetragonal space group P4₁ or P4₃, with unit-cell parameters a = b = 139.88, c = 73.37 Å. There were two homodimers in the asymmetric unit. A native data set was collected to 1.55 Å resolution and a data set suitable for MAD phasing was collected to 2.40 Å resolution on beamline BL40B2 at SPring-8.

Keywords: geranylgeranyl diphosphate synthase

Document Type: Research article

DOI: http://dx.doi.org/10.1107/S0907444903025496

Publication date: 2004-01-01