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This report describes the crystallization and X-ray diffraction analysis of a regulatory domain of the Toll-like receptor signalling adaptor TRIF/TICAM-1 and its SeMet-labelled mutant containing two additional Met residues. This domain is unrelated in sequence to any protein of known structure.

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To investigate the molecular basis of immune signalling initiated by the TIR domains of plant disease-resistance proteins, the crystallization and preliminary X-ray diffraction analyses of the TIR domains of three proteins involved in disease resistance in A. thaliana are reported.
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