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

Mareike Kurz, Inaki Iturbe-Ormaetxe, Russell Jarrott, Scott Leslie O'Neill, K Byriel, Jennifer Martin, Begona Heras

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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 angstrom, 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 angstrom using a copper anode and data from SeMet alpha-DsbA1 crystals were recorded to 2.45 angstrom resolution using a chromium anode.
Original languageEnglish
Pages (from-to)94 - 97
Number of pages4
Journal Acta Crystallographica Section F: Structural Biology Communications
Publication statusPublished - 2008
Externally publishedYes

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