Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of the FeoB G domain from Methanococcus jannaschii
Author(s) -
Köster Stefan,
Kühlbrandt Werner,
Yildiz Özkan
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109019216
Subject(s) - methanococcus , tetragonal crystal system , crystallization , crystallography , solvent , diffraction , chemistry , materials science , biochemistry , crystal structure , organic chemistry , gene , escherichia coli , physics , optics
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 Å 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.