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Monitoring protein crystallization by dynamic light scattering
Author(s) -
Mikol V.,
Hirsch E.,
Giegé R.
Publication year - 1989
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(89)81616-3
Subject(s) - supersaturation , crystallization , light scattering , dynamic light scattering , protein crystallization , scattering , crystallography , materials science , chemical physics , chemistry , chemical engineering , analytical chemistry (journal) , optics , chromatography , physics , nanotechnology , organic chemistry , engineering , nanoparticle
Crystallization of lysozymes induced by temperature lowering has been monitored by dynamic light scattering from the onset of supersaturation to the growth of protein crystals up to a noticeable size (150–200 μm). The apparent size of the scatterers was found to increase up to a maximum value as supersaturation proceeded, then to decrease down to its initial value. Apparitions of crystals (20–30 μm) were observed during this decrease. Light scattering is thus proved to be a sensitive technique to follow protein crystallization and to provide useful information on the process.