| The 'phase problem' is central to X-ray crystallography, and multiwavelength anomalous diffraction (MAD) provides an elegant and broadly accessible solution. In the first part, the use of MAD at the xenon L3 edge is explored, as an alternative to the well established selenium K-edge phasing. In the second part, the structure of the bacterial protein Vibrio cholerae LuxQ, part of a two component signaling system involved in quorum sensing, is solved and analyzed.; Keywords: anomalous scattering, x-ray diffraction, phasing, protein structure. |
