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Surface relaxation in protein crystals.

S Boutet1, I K Robinson, Z W Hu

  • 1Department of Physics, University of Illinois, Urbana, IL 61801, USA.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|January 7, 2003
PubMed
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Surface x-ray diffraction revealed surface roughness and top layer contraction in horse spleen ferritin crystals. Unexpected peaks were explained by multiple scattering, suggesting future hydration studies.

Area of Science:

  • Biophysics
  • Crystallography
  • Materials Science

Background:

  • Horse spleen ferritin is a cellular iron-storage protein crucial for iron homeostasis.
  • Understanding protein crystal surface properties is vital for structural biology and materials science.
  • Surface x-ray diffraction (SXD) is a powerful technique for probing crystal surfaces at the atomic level.

Purpose of the Study:

  • To characterize the surface structure of horse spleen ferritin crystals using SXD.
  • To investigate surface roughness and layer spacing of ferritin crystals.
  • To analyze anomalous peak occurrences in crystal rocking curves.

Main Methods:

  • Surface x-ray diffraction (SXD) measurements were conducted on (111) growth faces of horse spleen ferritin crystals.

Related Experiment Videos

  • Crystal truncation rods (CTRs) were measured to analyze surface structure.
  • Rocking curves were analyzed to identify and explain unexpected diffraction peaks.

    • Main Results:

    • SXD analysis revealed a surface roughness of 48+/-4.5 Å for the ferritin crystals.
    • A top layer spacing contraction of 3.9+/-1.5% was determined.
    • Unexpected extra peaks in rocking curves were attributed to multiple scattering phenomena.

    Conclusions:

    • SXD provides quantitative insights into the surface structure of protein crystals like ferritin.
    • The findings highlight the importance of considering multiple scattering in diffraction analysis.
    • This methodology holds potential for studying hydration effects during protein crystal growth.