Abstract
Autotransporters (ATs) are proteins that deliver effectors (the passenger domain) to the surface of Gram-negative bacteria by the type V secretion pathway. The passenger domain of BrkA, a Bordetella pertussis autotransporter mediating serum resistance and adherence, was cloned in a pET expression system and overexpressed in Escherichia coli. The gene product was correctly refolded, purified to homogeneity and crystallized. The crystals diffracted to 2.8 Å resolution. The space group was assumed to be P41212, with unit-cell parameters a = b = 108.19, c = 115.35 Å. © 2009 International Union of Crystallography. All rights reserved.
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Zhao, L., Nguyen, N. T., Fernandez, R. C., & Murphy, M. E. P. (2009). Crystallographic characterization of the passenger domain of the Bordetella autotransporter BrkA. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(6), 608–611. https://doi.org/10.1107/S174430910901642X
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