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Dynamic light scattering studies of the aggregation of lysozyme under crystallization conditions
Author(s) -
Skouri Mohammed,
Delsanti Michel,
Munch Jean-Pierre,
Lorber Bernard,
Giegé Richard
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81391-k
Subject(s) - lysozyme , supersaturation , crystallization , nucleation , scattering , light scattering , crystallography , protein crystallization , chemistry , dynamic light scattering , materials science , chemical physics , analytical chemistry (journal) , optics , chromatography , physics , biochemistry , nanotechnology , organic chemistry , nanoparticle
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° to 90°. 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 correlated with the nucleation step during protein crystallization.