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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2008-02, Vol.64 (2), p.94-97
• Main Authors: Kurz, M., Iturbe-Ormaetxe, I., Jarrott, R., O'Neill, S. L., Byriel, K. A., Martin, J. L., Heras, B.
• Format: Article
• Language: English
• Subjects: ANODES; CHROMIUM; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; COPPER; CRYSTALLIZATION; Crystallization Communications; Crystallography, X-Ray; CRYSTALS; DIFFRACTION; DIFFUSION; DsbA homologues; MOLECULES; Polymerase Chain Reaction; Protein Disulfide-Isomerases - chemistry; PROTEINS; Recombinant Proteins - chemistry; RESOLUTION; SPACE GROUPS; Wolbachia - chemistry; Wolbachia pipientis
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309108000055

α‐DsbA1 is one of two DsbA homologues encoded by the Gram‐negative α‐proteobacterium Wolbachia pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The α‐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 α‐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, β = 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 α‐DsbA1 crystals were recorded to 2.45 Å resolution using a chromium anode.