The structure of this molecule was solved at RapiData 2006 by Fabio Rinaldi from the lab of Beatriz Guimaraes at the LNLS (Brazilian Synchrotron Light Laboratory -- http://www.lnls.br/ [Notice the little word "English" in the upper right corner]).  Here is a description:

Structural Studies of the Disulfide Oxidoreductases DsbA from Xylella fastidiosa
Rinaldi, F. C. and Guimarães, B.G.
Laboratório Nacional de Luz Síncrotron LNLS - Campinas SP Brazil

The disulfide oxidoreductases (DsbA) are periplasmic proteins involved in disulfide bond formation. The DsbA's assist the folding of exported proteins containing disulfide bonds. Xylella fastidiosa is a phytopathogenic bacterium that causes serious diseases in a wide range of economically important crops. We are performing structural studies on the oxidoreductase DsbA from this organism.  We have solved the crystal structure of DsbA by the single-wavelength anomalous diffraction (SAD) method. The DsbA was labelled with selenomethionine (SeMet).  Mass spectrometry analysis showed that all three methionine residues were replaced by SeMet. X-ray diffraction data were collected in the X26-C protein crystallography beam line at the National Synchrotron Light Source (NSLS),
Brookhaven National Laboratory (BNL) during the course RapiData 2006. A data set of the SeMet-substituted form was collected to a resolution of 1.85Å and belonged to space group C2, with unit-cell parameters: a= 203.16 Å, b= 42.54 Å, c= 81.435 Å, ß= 96.15.  The selenium sub-structure (six sites) was solved using the program SHELXD. The phases calculated with the program SHARP/autoSHARP were sufficient for automatic tracing of over 93 % of the structure using the program ARP/wARP.  Further manual rebuilding was done and the three molecules present in the asymmetric unit had their structural refinement carried out with REFMAC.  The complete model was refined to a final R/Rfree of 0.196/0.233.