Hello all, Some crystal structures seem to contain a very low number of water molecules given their resolution (e.g 1 water for every 10 amino acid residues at 2.2Angstrom, whereas probably around 0.6 waters per residue is expected on average). I was wondering if anybody has any insights (or better: a good reference) into the precise reasons. Of course general data quality comes into mind, or using data-to-parameter ratio rather than resolution. But how about intrinsic properties the protein?
So my exact questions are: - How frequent is a very low number of visible waters observed? - What are the usual reasons? Cheers Filip Van Petegem -- Filip Van Petegem, PhD Assistant Professor The University of British Columbia Dept. of Biochemistry and Molecular Biology 2350 Health Sciences Mall - Rm 2.356 Vancouver, V6T 1Z3 phone: +1 604 827 4267 email: [email protected] http://crg.ubc.ca/VanPetegem/
