"X-Ray Structure Analysis of the Iron-Dependent Superoxide Dismutase from Mycobacterium tuberculosis at 2.0 Angstroms Resolution Reveals Novel Dimer-Dimer Interactions."

According to the authors' abstract of an article published in Journal of Molecular Biology, "The X-ray structure of the tetrameric iron-dependent superoxide dismutase from Mycobacterium tuberculosis has been refined to an R-factor of 0.167 and a correlation coefficient of 0.954 at 2.0 Angstrom resolution. The crystals are monoclinic P2(1) and have four subunits related by strong non-crystallographie 222 (or D-2) symmetry in the asymmetric unit. 198 of the 207 amino acids of each subunit are defined by the electron density which shows that they adopt the conserved fold of other iron- or manganese-dependent SODs. The structure can be divided into two domains, the N-terminal domain...

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