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

Authors
  • Nishio, Kazuya
  • Nodake, Yuichi
  • Hamada, Kensaku
  • Suto, Kyoko
  • Nakagawa, Noriko
  • Kuramitsu, Seiki
  • Miura, Keiko
Type
Published Article
Journal
Acta crystallographica. Section D, Biological crystallography
Publication Date
Jan 01, 2004
Volume
60
Issue
Pt 1
Pages
178–180
Identifiers
PMID: 14684922
Source
Medline
License
Unknown

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 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.

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