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

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.

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 Creators:
Cordes, Frank S., Author
Kraiczy, Peter, Author
Roversi, Pietro, Author
Skerka, Christine, Author
Kirschfink, Michael, Author
Simon, Markus1, Author           
Brade, Volker, Author
Lowe, Edward D., Author
Zipfel, Peter, Author
Wallich, Reinhard, Author
Lea, Susan M., Author
Affiliations:
1Metchnikoff Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243654              

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 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.

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Language(s): eng - English
 Dates: 2004
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: eDoc: 208348
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Title: Acta Crystallographica
Source Genre: Journal
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Pages: - Volume / Issue: D60 Sequence Number: - Start / End Page: 929 - 932 Identifier: -