Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain
Research output: Contribution to journal › Journal article › Research › peer-review
Tina Vognsen, Ingvar Rúnar Möller, Ole Kristensen
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.
|Journal||Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online|
|Issue number||Pt 1|
|Publication status||Published - 1 Jan 2011|
- Former Faculty of Pharmaceutical Sciences