title: Growth inhibition of lysozyme crystals at high hydrostatic pressure.
abstract: The influence of high hydrostatic pressures on the crystallization of hen egg-white lysozyme has been determined by growing lysozyme crystals with a capillary technique adapted to high pressure conditions and monitoring the residual protein concentration remaining in the supernatant. Pressure is found to reduce the rate of crystallization and to enhance the solubility of lysozyme in 1 M NaCl, pH 4.66. The volume change calculated from the latter result amounts to 12.5 ml/mol. This value is too small to be detectable by comparison of total molar volumes.
authors.affiliation: Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Gross
authors.forename: R
authors.initials: R
authors.lastname: Jaenicke
mesh_terms: D000818:Animals; D002645:Chickens; D003460:Crystallization; D006863:Hydrogen-Ion Concentration; D006874:Hydrostatic Pressure; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D009113:Muramidase