Crystallization and preliminary X-ray analysis ofSalmonellaFliI, the ATPase component of the type III flagellar protein-export apparatus

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Abstract
Most of the structural components making up the bacterial flagellum are translocated through the central channel of the growing flagellar structure by the type III flagellar protein-export apparatus in an ATPase-driven manner and are assembled at the growing end. FliI is the ATPase that drives flagellar protein export using the energy of ATP hydrolysis. FliI forms an oligomeric ring structure in order to attain maximum ATPase activity. In this study, FliI(Delta1-18), an N-terminally truncated variant of FliI lacking the first 18 residues, was purified and crystallized. Crystals were obtained using the hanging-drop vapour-diffusion technique with PEG 8000 as a precipitant. FliI(Delta1-18) crystals grew in the monoclinic space group P2(1), with unit-cell parameters a = 48, b = 73, c = 126 A, beta = 94 degrees, and diffracted to 2.4 A resolution. Anomalous difference Patterson maps of Os-derivative and Pt-derivative crystals showed significant peaks in their Harker sections, indicating that both derivatives are suitable for structure determination.