Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 P4(1) or P4(3), with unit-cell parameters a = b = 139.88, c = 73.37 A. There were two homodimers in the asymmetric unit. A native data set was collected to 1.55 A resolution and a data set suitable for MAD phasing was collected to 2.40 A resolution on beamline BL40B2 at SPring-8.
Expression, purification, crystallization and preliminary X-ray studies of geranylgeranyl diphosphate synthase from Thermus thermophilus HB8.,Nishio K, Nodake Y, Hamada K, Suto K, Nakagawa N, Kuramitsu S, Miura K Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):178-80. Epub 2003, Dec 18. PMID:14684922[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nishio K, Nodake Y, Hamada K, Suto K, Nakagawa N, Kuramitsu S, Miura K. Expression, purification, crystallization and preliminary X-ray studies of geranylgeranyl diphosphate synthase from Thermus thermophilus HB8. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):178-80. Epub 2003, Dec 18. PMID:14684922
