James:
Br MAD/SAD however, is not that complicated.
You can move to the Br edge (13476 eV) in the "Hutch" tab, 
and the run "optimize beam" just to be sure you have all the flux you can.

You do the fluorescence scan with the "Scan" tab in BLU-ICE and the 
recommended wavelengths will appear marked in the spectrum.  
Hitting "update" in the "collect" tab will copy these values over.

I recommend collecting TWO photon energies at the same time.  
One halfway between the recommended "peak" and "inflection" and 
another 300 eV away in either direction. 
Preferably higher in energy, unless you have more than ~200 mM Br 
(the crystal will absorb significantly more energy above the Br edge than below it).

The choice of whether or not to use inverse beam depends on your space group.  
If you have orthogonal symmetry axes, then you usually don't need inverse beam.  
(I.E. P4 -> use inverse beam; P422 -> don't have to)

At 13.5 keV, a typical protein crystal will reach the "Henderson limit" of 20 MGy in ~1.5 hours on 8.3.1.  This is where half of your diffraction spots will have been burned away.  Specific damage to particular atoms, such as active sites and heavy atom sites, can take place as much as ~7 times faster than this, so you need to start worrying about radiation damage after ~15 minutes.

I additionally recommend that you repeat your fluorescence scan (with the SAME crystal orientation) after your data collection is done, or perhaps at ~10 minute intervals.  If you see changes in the spectrum, then your Br site is probably falling off.  You can either move on to another crystal at that point, or try to use the "RIP" differences to solve the structure (by subtracting a "damaged" data set from a complete early data set).

-James