HI all. I am solving protein structure with 2.16A resolution. There are two chain in an asymmetric unit. I see that in one of the chain, many residues' density for side chains is incomplete and therefore results in poor density fit.
*I want to know your opinions for the approach I have taken. Figures relevant to each approach have been attached herewith.* *Case1*: There is no experimental density at all. Therefore, i have deleted side chains to Gly. *Case2*: Though there is incomplete density for Leu, it is enough to suggest its rotamer. In this case, as may be seen, i have just set occupancy for atoms without density(CG, CD1, CD2) to zero. Hopeful for the response. -- Vipul Panchal Senior Research Fellow, Respiratory disease and biology, CSIR-IGIB (M)-9540113372
