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

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Kurz, M
Iturbe-Ormaetxe, I
Jarrott, R
O'Neill, SL
Byriel, KA
Martin, JL
Heras, B
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2008
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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.

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Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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F64

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2

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Chemical sciences

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Biochemistry and cell biology not elsewhere classified

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