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

Journal article

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.

Authors: Cordes, F; Kraiczy, P; Roversi, P; Skerka, C; Kirschfink, M

• Publication status: Published
• Journal: Acta crystallographica. Section D, Biological crystallography
• Volume: 60
• Issue: Pt 5
• Pages: 929-932
• Publication date: 2004-05-01
• DOI: 10.1107/s090744490400472x
• EISSN: 1399-0047
• ISSN: 0907-4449
• Language: English
• Keywords: Escherichia coli; Selenium; Selenomethionine; Protein Conformation; Binding Sites; Bacterial Proteins; Borrelia burgdorferi; Crystallography, X-Ray; Membrane Proteins; Recombinant Proteins; Crystallization