http://skuld.bmsc.washington.edu/scatter/AS_form.html
Maybe useful to you. However, I would advise to do a fluorescence scan over the range given in the graph and then use chooch to provide the precise energies for your peak and inflection. If you have a large crystal don't expose all of it when you do the fluorescence scan but rather reserve a 'fresh' piece to do your actual data collection. F On Mar 6, 2012, at 1:09 PM, Deepthi wrote: > Hi > > I am trying to solve the structure of an engineered protein.The protein is > crystallized with Zn bound to it .We collected a 1.5A0 data. Molecular > Replacement didn't yield a good match for the protein. I want to try MAD > taking advantage of the Zn atoms in protein. I am not sure what wavelength > should i use to collect the diffraction data for Zn. any suggestions? > > Thank You > Deepthi > > -- > Deepthi
