Structure determination by multiple wavelength anomalous dispersion MAD at the Pr LIII edge

The use of longer X ray wavelengths in macromolecular crystallography has grown significantly over the past few years. The main reason for this increased use of longer wavelengths has been to utilize the anomalous signal from sulfur, providing a means for the experimental phasing of native proteins. Here, another possible application of longer X ray wavelengths is presented MAD at the LIII edges of various lanthanide compounds. A first experiment at the LIII edge of Pr was conducted on HZB MX beamline BL14.2 and resulted in the successful structure determination of the C terminal domain of a spliceosomal protein. This experiment demonstrates that LIII edges of lanthanides constitute potentially attractive targets for long wavelength MAD experiment