Neutron diffraction analysis of the solvent accessible volume in cubic insulin crystals.
The average contact distance between protein and solvent surface atoms in cubic insulin crystals has been determined from two sets of 15 A resolution neutron diffraction data. A contact distance between the water hydrogen sites and the protein surface that is significantly shorter than the average protein-water oxygen contact distance implies that many water molecules are oriented with hydrogen atoms pointed towards the protein surface. The shape of the protein/solvent interface is consistent with the protein envelope obtained from atomic co-ordinates.
Badger
J
J
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.
Kapulsky
A
A
Caspar
D L
DL
Korszun
R
R
D000818:Animals; D003461:Crystallography; D017666:Deuterium Oxide / Q000737:chemistry; D007328:Insulin / Q000737:chemistry*; D009502:Neutrons; D011487:Protein Conformation; D012542:Scattering, Radiation; D012997:Solvents; D013552:Swine; D014867:Water / Q000737:chemistry*
D007328:Insulin; D012997:Solvents; D014867:Water; D017666:Deuterium Oxide