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The ATPase domain of the membrane-anchored protease FtsH of E. coli has been crystallized and native data to 1.5 Å spacing have been collected using synchrotron radiation.

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The cell division protein DivIVA is predicted to be a coiled-coil, tropomyosin-like protein, that self-associates both in vivo and in vitro into oligomers of up to 10-12 monomers. A simple and quick screen for conditions supporting the stable oligomer structure has been developed revealing that DivIVA forms a homogeneous oligomer in the presence of PEGs (PEG 4K or PEG 8K and PEG 1K).
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