Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 2 (February 2008)


crystallization communications



Acta Cryst. (2008). F64, 94-97    [ doi:10.1107/S1744309108000055 ]

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

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

Abstract: [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 Å, [beta] = 107.0° and one molecule in the asymmetric unit (44% solvent content). X-ray data were recorded from native crystals to a resolution of 2.01 Å using a copper anode and data from SeMet [alpha]-DsbA1 crystals were recorded to 2.45 Å resolution using a chromium anode.

Keywords: DsbA homologues; Wolbachia pipientis.

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