Hi everyone, I'd like to add that tunable synchrotron beamlines are tending more and more to support Sufur-SAD on native proteins - in particular, there are dedicated long-wavelength beamlines (like I23 at Diamond).
And if radiation damage is the main concern, availability of multiple crystals (if one is in the lucky situation of getting many isomorphous ones of sufficient quality), can be exploited to get high multiplicity data by merging their anomalous diffraction intensities, see e.g.: Liu et al. (2012). Science 336, 1033. El Omari et al. (2014). Acta D 70, 2197. Best regards, Fabio
Hi Giuliana, if your crystal diffracts to 3 Å or better and you have at least one Cys/Met per 25 residues, put it on the home source and collect until the sulfur signal rises above the noise. Then solve by SAD. http://www3.imperial.ac.uk/xraycrystallography/learning/sulfur_sad <http://www3.imperial.ac.uk/xraycrystallography/learning/sulfur_sad> Andreas
-- Dr. rer. nat. Fabio Dall'Antonia European Molecular Biology Laboratory c/o DESY Notkestraße 85, Bldg. 25a D-22603 Hamburg phone: +49 (0)40 89902-178 fax: +49 (0)40 89902-149 e-mail: fabio.dallanto...@embl-hamburg.de
