Hello,

I am new to protein x-ray crystallography and recently I acquired some datasets 
that I have been attempting to solve.

When I process the diffraction data for a particular dataset that is 1.8 
Angstroms, I either get P21 or P212121 depending on the processing software I 
use (DIALS vs HKL2000). I solve both using molecular replacement in PHENIX and 
the density fits quite well for both. My LLG scores for both solutions were 
~1051 and the TFz scores were ~32.

The issue is, after modeling waters and being in the later stages of 
refinement, for both structures my Rfactors remain a bit high for the 
resolution. For the P212121 structure, they are a little lower Rwork: 0.2351 
and Rfree: 0.2861. For the P21 structure, they are Rwork: 0.2371 Rfree: 0.2739. 
I will say that I believe the density looks slightly better for the P212121 
structure, but it is also difficult to compare as they are both good.

I am wondering if anybody knows why this may be happening, as well as other 
statistics/modeling aspects I could investigate in order to figure this out. If 
some other statistics from processing/modelling or more information is needed 
to diagnose the issue, I would be happy to provide it here. I just did not want 
to make my inquiry too long.

Thank you in advance for your help.

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