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

نویسندگان

  • Frank S Cordes
  • Peter Kraiczy
  • Pietro Roversi
  • Christine Skerka
  • Michael Kirschfink
  • Markus M Simon
  • Volker Brade
  • Edward D Lowe
  • Peter Zipfel
  • Reinhard Wallich
  • Susan M Lea
چکیده

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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عنوان ژورنال:
  • Acta crystallographica. Section D, Biological crystallography

دوره 60 Pt 5  شماره 

صفحات  -

تاریخ انتشار 2004