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: | , , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2004
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| 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 |
| 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 |
| Summary: | 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. |
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| Item Description: | Gesehen am 26.02.2021 |
| Physical Description: | Online Resource |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/S090744490400472X |