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Liquidsolid transition in nuclei of protein crystals Aleksey Lomakin, Neer Asherie, and George B. Benedek*
 

Summary: Liquid­solid 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 main-
tain 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 be-
yond a critical size (about a few hundred particles) crystal nucle-
ation becomes possible.
The inability to produce high-quality crystals is currently a
major hurdle in determining the 3D x-ray structure of
proteins (1). In addition, the crystallization of proteins is in-
volved in diseases such as human genetic cataract (2). It is
therefore important to improve the understanding of the ther-

  

Source: Asherie, Neer - Departments of Physics & Biology, Yeshiva University
Benedek, George B. - Department of Physics, Massachusetts Institute of Technology (MIT)

 

Collections: Biology and Medicine; Physics