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Purification, crystallization and preliminary X-ray diffraction analysis of the FeoB G domain from Methanococcus jannaschii

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Köster,  Stefan
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Yildiz,  Özkan       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Köster, S., Kühlbrandt, W., & Yildiz, Ö. (2009). Purification, crystallization and preliminary X-ray diffraction analysis of the FeoB G domain from Methanococcus jannaschii. Acta Crystallographie Section F Structural Biology and Crystallization Communications, F65(7), 684-687. doi:10.1107/S1744309109019216.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D795-8
Abstract
The transmembrane protein FeoB plays a key role in ferrous iron acquisition in prokaryotes. The N-terminal domain of FeoB from Methanococcus jannaschii was overproduced, purified to homogeneity and crystallized in the presence of GTP and magnesium. The native protein crystallized in a tetragonal space group and the crystals diffracted to beyond 2.2 Å resolution, with unit-cell parameters a = b = 84.77, c = 137.90 Å. The Matthews coefficient and the solvent content were estimated to be 2.65 Å3 Da-1 and 53.64%, respectively, which corresponds to the presence of two molecules per asymmetric unit. To obtain initial phases, selenomethionyl-substituted protein was overproduced, purified and crystallized