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)
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
Publication date: 2004-01-01