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Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.
Kurz, M; Iturbe-Ormaetxe, I; Jarrott, R; O'Neill, S L; Byriel, K A; Martin, J L; Heras, B.
Affiliation
  • Kurz M; Institute for Molecular Bioscience and ARC Special Research Centre for Functional and Applied Genomics, University of Queensland, St Lucia, QLD 4072, Australia.
Article in En | MEDLINE | ID: mdl-18259058
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Disulfide-Isomerases / Wolbachia Language: En Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Year: 2008 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Disulfide-Isomerases / Wolbachia Language: En Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Year: 2008 Document type: Article