Dear Michelle, this is not strange at all. You simply have a MR solution that refers to a different origin. You cannot display the original model plus the MR solution in the same coordinate system (with respect to the same origin). Of course they clash.
Greetings Marius > Dear all, > > I refined a protein structure in the space group P6(1)22, with one > copy in the > asymmetric unit, resolution ~1.8 A, Rwork=0.20, Rfree=0.22. > Then I tried to feed Phaser (version 1.3.3) with this structure. It > found > quickly a very prominent solution, but the first euler angle is 180 > instead of 0 > degrees (the others are 0, as well as the fractional coordinates). > This solution > is not symmetry-related with the structure that I used as search > model: indeed, > there are a lot of clashes. However, when I refine this solution, I > obtain > immediately R factors as good as the search model, and also the > electron density > map looks perfect. Of course, I used the same reflections file to > refine the > initial structure and the MR solution rotated of 180 degrees. > > How can I explain this? The analysis with Truncate (moments and > cumulative > intensity distribution) don't suggest any twinning, as well as the > Padilla-Yeates test. Is it possible, that I refined the structure in > the wrong > space group? > > Thank you in advance, > > Michele Lunelli
