Expression, purification, crystallization and preliminary X-ray studies of geranylgeranyl diphosphate synthase from Thermus thermophilus HB8.
Acta Crystallogr D Biol Crystallogr
; 60(Pt 1): 178-80, 2004 Jan.
Article
em En
| MEDLINE
| ID: mdl-14684922
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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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Thermus thermophilus
/
Alquil e Aril Transferases
Idioma:
En
Ano de publicação:
2004
Tipo de documento:
Article