title: Neutron diffraction analysis of the solvent accessible volume in cubic insulin crystals.
abstract: 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.
authors.affiliation: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.
authors.forename: J
authors.initials: J
authors.lastname: Badger
authors.forename: A
authors.initials: A
authors.lastname: Kapulsky
authors.forename: D L
authors.initials: DL
authors.lastname: Caspar
authors.forename: R
authors.initials: R
authors.lastname: Korszun
mesh_terms: 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*
chemical_list: D007328:Insulin; D012997:Solvents; D014867:Water; D017666:Deuterium Oxide