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Crystallization and preliminary crystallographic analysis of BbCRASP-1, a complement regulator-aquiring surface protein of Borrelia burgdorferi

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Simon,  Markus
Metchnikoff Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Cordes, F. S., Kraiczy, P., Roversi, P., Skerka, C., Kirschfink, M., Simon, M., et al. (2004). Crystallization and preliminary crystallographic analysis of BbCRASP-1, a complement regulator-aquiring surface protein of Borrelia burgdorferi. Acta Crystallographica, D60, 929-932.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-946A-8
Abstract
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 Å as well as selenomethionine MAD data to 3.2 Å resolution have been collected. The selenium substructure has been solved and initial phases have been refined to 3.0 Å by density-modification methods. Model building and refinement are under way.