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

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 A resolution, with unit-cell parameters a = b = 84.77, c = 137.90 A. The Matthews coefficient and the solvent content were estimated to be 2.65 A(3) 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.

SUBMITTER: Koster S

PROVIDER: S-EPMC2705634 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature

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

Köster Stefan S Kühlbrandt Werner W Yildiz Ozkan O

Acta crystallographica. Section F, Structural biology and crystallization communications 20090627 Pt 7

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 A resolution, with unit-cell parameters a = b = 84.77, c = 137.90 A. The Matthews coefficient and the solvent content were estimated to be 2.65 A(3) ...[more]

PMID: 19574639

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