Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.
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.
Kurz
M
M
Institute for Molecular Bioscience and ARC Special Research Centre for Functional and Applied Genomics, University of Queensland, St Lucia, QLD 4072, Australia.
Iturbe-Ormaetxe
I
I
Jarrott
R
R
O'Neill
S L
SL
Byriel
K A
KA
Martin
J L
JL
Heras
B
B
D003460:Crystallization; D018360:Crystallography, X-Ray; D016133:Polymerase Chain Reaction; D019704:Protein Disulfide-Isomerases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D020577:Wolbachia / Q000737:chemistry*
D011994:Recombinant Proteins; D019704:Protein Disulfide-Isomerases