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Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain.

ABSTRACT: The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6?Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a=b=89.84, c=70.02?Å. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial phases were obtained by molecular replacement.

SUBMITTER: Vognsen T 

PROVIDER: S-EPMC3079970 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain.

Vognsen Tina T   Möller Ingvar Rúnar IR   Kristensen Ole O  

Acta crystallographica. Section F, Structural biology and crystallization communications 20101221 Pt 1

The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6 Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a=b=89.84, c=70.02 Å. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial  ...[more]

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