title: Fractal aggregates in protein crystal nucleation.
abstract: Monte Carlo simulations of homogeneous nucleation for a protein model with an exceedingly short-ranged attractive potential yielded a nonconventional crystal nucleation mechanism, which proceeds by the formation of fractal, low-dimensional aggregates followed by a concurrent collapse and increase of the crystallinity of these aggregates to become compact ordered nuclei. This result corroborates a recently proposed two-step mechanism for protein crystal nucleation from solution.
authors: Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803-1804, USA. binchen@lsu.edu
authors: Bin
authors: B
authors: Chen
authors: Ricky B
authors: RB
authors: Nellas
authors: Samuel J
authors: SJ
authors: Keasler
mesh_terms: D003198:Computer Simulation; D003460:Crystallization; D008956:Models, Chemical; D009010:Monte Carlo Method; D011506:Proteins / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry
chemical_list: D011506:Proteins; D012996:Solutions