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Related Experiment Videos

Dissipating step bunches during crystallization under transport control.

Hong Lin1, S-T Yau, Peter G Vekilov

  • 1Center for Microgravity and Materials Research, University of Alabama in Huntsville, Huntsville, Alabama 35899, USA.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|April 12, 2003
PubMed
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Equidistant step trains are stable during protein crystallization, contrary to prior beliefs. Controlling nucleation sites allows for patterned or smoothened crystal surfaces.

Area of Science:

  • Crystallization dynamics
  • Surface science
  • Protein crystallization

Background:

  • Equidistant step trains were previously considered unstable during crystal growth.
  • Spatiotemporal patterns of growth steps were widely believed to be ubiquitous.

Purpose of the Study:

  • To investigate the stability of equidistant step trains during protein crystallization.
  • To elucidate the mechanisms behind step bunching and surface morphology.
  • To explore methods for controlling crystal surface patterns.

Main Methods:

  • Atomic force microscopy (AFM) was used to monitor step dynamics during ferritin and apoferritin crystallization.
  • Analysis of step velocity and density variations.
  • Numerical modeling to support experimental observations.

Related Experiment Videos

Main Results:

  • Step variations in velocity and density were uncorrelated, indicating a lack of long-range attraction.
  • Nucleation of new layers is chaotic, coupled to bulk transport, and occurs at facet edges.
  • Step bunches self-organize through competition for solution supply and decay over distance.
  • Equidistant step trains are the stable kinetic state for transport-controlled crystallization with non-interacting steps.

Conclusions:

  • Step bunches arise primarily during new layer nucleation, not as a stable state.
  • Controlling local nucleation sites offers a method for patterning or smoothing crystal surfaces.
  • The findings challenge previous assumptions about step train stability in crystallization.