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Macromolecular complexes in crystals and solutions.

Evgeny Krissinel1

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Crystal packing may misrepresent weak macromolecular interactions (K(d) ≥ 100 µM), potentially affecting up to 20% of protein dimers. Complementary noncrystallographic studies are crucial for accurate structural analysis of weakly bound complexes.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Macromolecular interactions are fundamental to biochemical processes.
  • Crystal packing is a common method for determining macromolecular structures.
  • Existing methods for analyzing crystal packing may yield inaccurate results.

Purpose of the Study:

  • To discuss existing methods for analyzing macromolecular interactions in crystal packing.
  • To investigate the relationship between natural (in-solvent) and crystallized assemblies.
  • To identify conditions where crystal packing may misrepresent macromolecular complexes.

Main Methods:

  • Review of existing methods for analyzing macromolecular interactions in crystal packing.
  • Computational analysis of weak interactions and their likelihood of being lost during crystallization.
  • Estimation of misrepresentation likelihood for protein dimers in the Protein Data Bank (PDB).

Main Results:

  • Weak interactions (K(d) ≥ 100 µM) have a considerable chance of being lost during crystallization.
  • Crystal packing can misrepresent macromolecular complexes and interactions, particularly for weak binders.
  • An estimated 20% of protein dimers in the PDB show a >50% likelihood of misrepresentation.

Conclusions:

  • Crystal packing may not accurately reflect natural macromolecular assemblies for weakly bound complexes.
  • Complementary noncrystallographic studies are essential for accurate structural insights into weakly interacting systems.
  • Understanding these limitations is vital for interpreting structural data and biochemical processes.