The SecA translocation ATPase is the engine which powers the ATP-driven extrusion of secreted proteins from the eubacterial cytoplasm. The protein can adopt a soluble form and a membrane-inserted form. We crystallized the soluble form, and, using X-ray diffraction data collected at CHESS and at other synchrotron facilities, determined its 3D-structure. Crystallographic refinement is near completion, and a manuscript is in preparation.
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