Enhancement of uniaxial magnetic anisotropy in Fe thin films grown on GaAs(001) with an MgO underlayer

The understanding and control of anisotropy in Fe films grown on cubic systems such as GaAs and MgO has been of interest from the point of view of applications in devices. We report magnetic anisotropy studies on Fe/GaAs(001) and Fe/MgO/GaAs(001) prepared by pulsed laser deposition. In Fe/GaAs(001), magneto optical Kerr effect (MOKE) measurements revealed a dominant uniaxial anisotropy for Fe thickness less than 20 monolayers (ML) and this was confirmed by ferromagnetic resonance (FMR) studies. Multiple steps in the hysteresis loops were observed for Fe films of thickness 20 and 25 ML. Whereas, in Fe/MgO/GaAs(001), even at 25 ML of Fe, the uniaxial anisotropy remained dominant. The anisotropy constants obtained from FMR spectra have shown that the relative strength of uniaxial anisotropy is higher as compared to the cubic anisotropy constant in the case of Fe/MgO/GaAs(001). (C) 2011 American Institute of Physics. doi:10.1063/1.3556941]

The biological and structural characterization of Mycobacterium tuberculosis UvrA provides novel insights into its mechanism of action

Mycobacterium tuberculosis is an extremely well adapted intracellular human pathogen that is exposed to multiple DNA damaging chemical assaults originating from the host defence mechanisms. As a consequence, this bacterium is thought to possess highly efficient DNA repair machineries, the nucleotide excision repair (NER) system amongst these. Although NER is of central importance to DNA repair in M. tuberculosis, our understanding of the processes in this species is limited. The conserved UvrABC endonuclease represents the multi-enzymatic core in bacterial NER, where the UvrA ATPase provides the DNA lesion-sensing function. The herein reported genetic analysis demonstrates that M. tuberculosis UvrA is important for the repair of nitrosative and oxidative DNA damage. Moreover, our biochemical and structural characterization of recombinant M. tuberculosis UvrA contributes new insights into its mechanism of action. In particular, the structural investigation reveals an unprecedented conformation of the UvrB-binding domain that we propose to be of functional relevance. Taken together, our data suggest UvrA as a potential target for the development of novel anti-tubercular agents and provide a biochemical framework for the identification of small-molecule inhibitors interfering with the NER activity in M. tuberculosis.