title: Dynamic light scattering studies of the aggregation of lysozyme under crystallization conditions.
abstract: The intensity autocorrelation functions of light scattered by lysozyme solutions under pre-crystallization conditions in NaCl-containing media were recorded at scattering angles from 20 degrees to 90 degrees. The measurements, conducted on freshly prepared protein solutions supersaturated more than 3-fold, indicate the simultaneous presence of two scatterer populations which can be assigned to individual protein molecules and to large particles. When solutions are undersaturated, or slightly supersaturated, light scattering only reveals the presence of the small scatterers. In the supersaturated medium, where aggregates were detected, lysozyme crystals grew in a time-span of 1-3 days after the scattering experiments. These results are medium, where aggregates were detected, lysozyme crystals grew in a time-span of 1-3 days after the scattering experiments. These results are correlated with the nucleation step during protein crystallization.
authors.affiliation: Laboratoire d'Ultrasons et de Dynamique des Fluides Complexes, URA 851 du CNRS, Université Louis Pasteur, Strasbourg, France.
authors.forename: M
authors.initials: M
authors.lastname: Skouri
authors.forename: M
authors.initials: M
authors.lastname: Delsanti
authors.forename: J P
authors.initials: JP
authors.lastname: Munch
authors.forename: B
authors.initials: B
authors.lastname: Lorber
authors.forename: R
authors.initials: R
authors.lastname: Giegé
mesh_terms: D000818:Animals; D002645:Chickens; D003460:Crystallization; D008027:Light; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification; D012542:Scattering, Radiation; D012996:Solutions
chemical_list: D012996:Solutions; D009113:Muramidase