Xenopus laevis IKKβ was expressed in insect cells and purified to homogeneity using Ni-affinity, ion exchange and gel filtration chromatography. It was crystallized at 4°C in polyethylene glycol (PEG) 6000 and K/Na phosphate for the P1 and I4122 crystals, respectively. The structure was determined by multi-wavelength anomalous diffraction (MAD) of the selenomethionyl protein.
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Structural Determination of Xenopus laevis IKKβ
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Cells
Gel filtration chromatography
Ikkβ
Insect
Ion exchange
Phosphate
Polyethylene glycol 6000
Protein
Xenopus laevis
Corresponding Organization :
Other organizations : Cornell University, University of California, San Diego, Ono Pharmaceutical (United States), Merck Serono (Switzerland)
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Variable analysis
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- Xenopus laevis IKKβ expression in insect cells
- Purification of Xenopus laevis IKKβ using Ni-affinity, ion exchange and gel filtration chromatography
- Crystallization of Xenopus laevis IKKβ at 4°C in polyethylene glycol (PEG) 6000 and K/Na phosphate for the P1 and I4122 crystals, respectively
- Determination of the structure of Xenopus laevis IKKβ by multi-wavelength anomalous diffraction (MAD) of the selenomethionyl protein
- Purification of Xenopus laevis IKKβ to homogeneity
- Crystallization conditions (temperature, PEG 6000, K/Na phosphate)
- Selenomethionyl protein used for MAD experiments
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