Hydration in protein crystallography.
Water in close proximity to the protein surface is fundamental to protein folding, stability, recognition and activity. Protein structures studied by diffraction methods show ordered water molecules around some charged, polar, and non-polar (hydrophobic) amino acids, although the later are only observed when they are at the interface between symmetry related molecules in the crystal. Water networks surrounding the protein have been observed for small proteins. Crystallographically observed water molecules are referred to as bound structural water molecules. During crystallographic data analysis, bound water molecules are often treated as though they belong to the protein. Recent developments in the treatment of the bulk solvent contribution to the low order diffraction data allow a better evaluation of the surface structure of the protein and a better localization of bound waters. The mobility of bound waters is studied by means of temperature and occupancy factors. The bulk solvent has relatively large disorder (liquid like) which is represented by liquidity factors. Within this context water layers surrounding the protein have little mobility.
Schoenborn
B P
BP
Los Alamos National Laboratory, New Mexico, USA.
Garcia
A
A
Knott
R
R
D055592:Biophysical Phenomena; D001703:Biophysics; D003461:Crystallography / Q000379:methods*; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry*; D012997:Solvents; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D011506:Proteins; D012997:Solvents; D014867:Water