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

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 (BbCRAS...

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Main Authors: Cordes, Frank (Author) , Kraiczy, Peter (Author) , Roversi, Pietro (Author) , Skerka, Christine (Author) , Kirschfink, Michael (Author) , Simon, Markus M. (Author) , Brade, Volker (Author) , Lowe, Edward D. (Author) , Zipfel, Peter F. (Author) , Wallich, Reinhard (Author) , Lea, Susan M. (Author)
Format: Article (Journal)
Language:English
Published: 2004
In: Acta crystallographica. Section D, Biological crystallography
Year: 2004, Volume: 60, Issue: 5, Pages: 929-932
ISSN:0907-4449
DOI:10.1107/S090744490400472X
Online Access:Verlag, lizenzpflichtig, Volltext: https://dx.doi.org/10.1107/S090744490400472X
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Author Notes:Frank S. Cordes, Peter Kraiczy, Pietro Roversi, Christine Skerka, Michael Kirschfink, Markus M. Simon, Volker Brade, Edward D. Lowe, Peter Zipfel, Reinhard Wallich and Susan M. Lea

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520 |a 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. 
650 4 |a Bacterial Proteins 
650 4 |a Binding Sites 
650 4 |a Borrelia burgdorferi 
650 4 |a Crystallization 
650 4 |a Crystallography, X-Ray 
650 4 |a Escherichia coli 
650 4 |a Membrane Proteins 
650 4 |a Protein Conformation 
650 4 |a Recombinant Proteins 
650 4 |a Selenium 
650 4 |a Selenomethionine 
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