ABSTRACT
Communicated by Ramaswamy H. Sarma.
Subject(s)
Solutions/chemistry , Thermolysin/chemistry , Crystallization/methods , Crystallography, X-Ray/methods , Models, Molecular , Protein ConformationABSTRACT
Solutions of lysozyme in heavy water were studied by small-angle neutron scattering (SANS) at concentrations of 40, 20 and 10â mgâ ml-1 with and without the addition of precipitant, and at temperatures of 10, 20 and 30°C. In addition to the expected protein monomers, dimeric and octameric species were identified in solutions at the maximum concentration and close to the optimal conditions for crystallization. An optimal temperature for octamer formation was identified and both deviation from this temperature and a reduction in protein concentration led to a significant decrease in the volume fractions of octamers detected. In the absence of precipitant, only monomers and a minor fraction of dimers are present in solution.
