Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.

نویسندگان

  • M Kurz
  • I Iturbe-Ormaetxe
  • R Jarrott
  • S L O'Neill
  • K A Byriel
  • J L Martin
  • B Heras
چکیده

alpha-DsbA1 is one of two DsbA homologues encoded by the Gram-negative alpha-proteobacterium Wolbachia pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The alpha-DsbA1 protein is thought to be important for the folding and secretion of Wolbachia proteins involved in the induction of reproductive distortions. Crystals of native and SeMet alpha-DsbA1 were grown by vapour diffusion and belong to the monoclinic space group C2, with unit-cell parameters a = 71.4, b = 49.5, c = 69.3 A, beta = 107.0 degrees and one molecule in the asymmetric unit (44% solvent content). X-ray data were recorded from native crystals to a resolution of 2.01 A using a copper anode and data from SeMet alpha-DsbA1 crystals were recorded to 2.45 A resolution using a chromium anode.

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عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology and crystallization communications

دوره 64 Pt 2  شماره 

صفحات  -

تاریخ انتشار 2008