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Borrelia burgdorferi is the causative agent of Lyme disease. Serum-resistant strains of the pathogen are able to reduce the host's immune response to infection by recruiting fluid-phase complement regulators from the serum. B. burgdorferi complement regulator-acquiring surface protein-1 (BbCRASP-1) binds factor H and factor-H-like protein-1 to the bacterial surface, where they actively down-regulate complement response. Crystals of native and selenomethionine-substituted BbCRASP-1 have been obtained and a native data set to 2.7 A as well as selenomethionine MAD data to 3.2 A resolution have been collected. The selenium substructure has been solved and initial phases have been refined to 3.0 A by density-modification methods. Model building and refinement are under way.

Original publication




Journal article


Acta Crystallogr D Biol Crystallogr

Publication Date





929 - 932


Bacterial Proteins, Binding Sites, Borrelia burgdorferi, Crystallization, Crystallography, X-Ray, Escherichia coli, Membrane Proteins, Protein Conformation, Recombinant Proteins, Selenium, Selenomethionine