Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):929-32. Epub 2004 Apr 21.

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

Cordes FS, Kraiczy P, Roversi P, Skerka C, Kirschfink M, Simon MM, Brade V, Lowe ED, Zipfel P, Wallich R, Lea SM.

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Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England.

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 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.

PMID:: 15103142; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Semet Derivative Of Bbcrasp-1 From Borrelia Burgdorferi

PDB: 1W3Z

Source: Borrelia burgdorferi ZS7

Method: X-Ray Diffraction

Resolution: 3.2 Å

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

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