Liquid-solid transition in nuclei of protein crystals
Aleksey Lomakin, Neer Asherie and George B. Benedek *
Department of Physics, Center for Materials Science and Engineering and Material Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139-4307
Contributed by George B. Benedek, July 1, 2003
It is generally assumed that crystallization begins with a small, crystalline nucleus. For proteins this paradigm may not be valid. Our numerical simulations show that under conditions typically used to produce protein crystals, small clusters of model proteins (particles with short-range, attractive interactions) cannot maintain a crystalline structure. Protein crystal nucleation is therefore an indirect, two-step process. A nucleus first forms and grows as a disordered, liquid-like aggregate. Once the aggregate grows beyond a critical size (about a few hundred particles) crystal nucleation becomes possible.
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