Hello everyone,

I have a few crystals to be x-rayed next week. Before that I hope to get a clear idea about what I am doing (I am new to anomalous scattering). 

Facts:

1. The crystal is a protein co-crystallized with a ligand
2. The protein structure is known.
3. The ligand has a heavy atom bromide (absorption K-egde=13.47Kev)
4. Data resolution is ~3 angstrom

Goals:

1. Locate the bromide position
2. Locate and refine the ligand

Questions:

1. Do I need to carry out MAD experiment at 3 wavelengths or there is some other easier way since the protein structure is known (I am not expecting big change of the protein structure     itself)?
2. Assuming I have the MAD data, what should I do next using phenix to achieve the two goals listed above? Here are some thoughts:
• Using phenix.hyss to locate the anomalous scatterers 
• Using phenix.autobuild to build the protein model (which data set to use?)
• Using coot to add ligands to the protein structure (Is the relative position between the protein and the ligand known based on phenix.hyss and phenix.autobuild?)
• Using phenix.refine to refine the ligand+protein complex

Thank you all for reading this.