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Structures of the EAL domain of the E. coli direct oxygen sensor show the active site in a nonproductive conformation that has implications for the regulatory mechanism.

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The crystal structure of the N-terminal part of T. thermophilus DnaJ unexpectedly showed an ordered GF domain and guided the design of a construct enabling the first structure determination of a complete DnaJ cochaperone molecule. By combining the crystal structures with spin-labelling EPR and cross-linking in solution, a dynamic view of this flexible molecule was developed.
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