I have this question. For exmaple, a protein could be crystallized in two
crystal forms. Two crystal form have same space group, and 1 molecule/asymm.
One crystal form diffracts to 3A with 50% solvent; and the other diffracts to
3.6A with 80% solvent. The cell volume of 3.6A crystal must be 5/2=2.5 times
larger because of higher solvent content. If both data collecte to same
completeness (say 100%), 3.6A data actually have higher data/parameter ratio,
5/2/(3.6/3)**3= 1.45 times to 3A data. For refinement, better data/parameter
should give more accurate structure, ie. 3.6A data is better. But higher
resolution should give a better resolved electron density map. So which crystal
form really give a better (more reliable and accurate) protein structure?
