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Water structure in cubic insulin crystals.

J Badger1, D L Caspar

  • 1Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.

Proceedings of the National Academy of Sciences of the United States of America
|January 15, 1991
PubMed
Summary

Researchers mapped solvent electron density in insulin crystals, revealing nonrandom water molecule arrangements extending beyond the protein surface. This ordering may explain hydration forces and long-range water interactions in biological structures.

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Proteins·2005

Area of Science:

  • Structural biology
  • Biophysics
  • Crystallography

Background:

  • The solvent, primarily water, occupies a significant volume (65%) within protein crystal structures.
  • Understanding solvent organization is crucial for interpreting protein-ligand interactions and crystal packing.

Purpose of the Study:

  • To map the electron density distribution of solvent in a cubic insulin crystal structure.
  • To investigate the arrangement and ordering of water molecules in the solvent space.

Main Methods:

  • Utilized 1.7-Å resolution diffraction data from a cubic insulin crystal.
  • Employed an iterative difference Fourier method with the known protein structure as a refinement restraint.
  • Initiated refinement with protein phases and a flat solvent model, iteratively updating phases based on the difference map.

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Main Results:

  • Successfully mapped the solvent electron density distribution within the insulin crystal.
  • Observed significant fluctuations in solvent density, indicating nonrandom arrangements of water molecules.
  • Demonstrated that water molecule ordering extends several layers beyond the protein's hydration shell.

Conclusions:

  • The iterative difference Fourier method reliably determines solvent density, even within the data's noise level.
  • Nonrandom solvent ordering suggests a role in hydration forces and long-range water-dependent interactions.
  • Findings provide insights into the physical basis of interactions between hydrophilic surfaces and solvent behavior in biological systems.