I hope it's OK if I chime in with this problem as well. I am working with a site-directed mutant of a commonly studied protein in our lab. It crystallize in P3121 and its unit cell is doubled along the c axis relative to a unit cell (P3221) that we have commonly seen with other mutants (the edges are roughly 55 x 55 x 88 or 55 x 55 x 176). Xtriage also picked up the pseuotranslational symmetry (0, 0, 0.5), which is not surprising given the unit cell dimensions. I was aware of the problem with weak and strong reflectiions, but that is not so obvious in our case. In HKLview one can see that in layers perpendicular to the c* axis, strong and weak reflections alternate out to about 8 Å, but the rest of the data (to 2.6 Å) appears - at least visibly - to be roughly consistent in intensity. Certainly when looking at the h0l or 0kl planes, there isn't any obvious alternation at higher resolution. We quickly obtained a model by molecular replacement but have stalled in refinement at an R/ Rfree of 30/38 (we have not tried TLS yet). The most obvious difficulty with the model is seen using density fit analysis in coot - one domain of one of the subunits in the asymmetric unit (related by translation NCS to the other) has weak density. Maybe this is just the luck of the draw - a crystal whose contents include 50% well ordered subunits and 50% not well ordered, but I'm curious if there is something obvious we should be trying. By the way, xtriage found no evidence of twinning, and the data also passed muster with dataman (Padilla-Yeates) and Todd Yeates' server. Thanks in advance, Arthur Glasfeld Department of Chemistry Reed College P.S. If anyone is interested I can send a figure with the hklview layers perpendicular to c* (hk0, hk1, hk2, hk3, hk4, hk5)