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Related Experiment Videos

New developments in phase refinement

J P Abrahams1, R A De Graaff

  • 1Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, The Netherlands. Abrahams@chem.leidenuniv.nl

Current Opinion in Structural Biology
|November 18, 1998
PubMed
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X-ray crystallography faces challenges with missing crystal phase information. Recent advancements in direct methods and automated refinement techniques are improving phase determination for small molecules and proteins.

Area of Science:

  • Crystallography
  • Structural Biology
  • Biophysics

Background:

  • X-ray crystallography is a powerful technique for determining the 3D structure of molecules.
  • A critical challenge in X-ray crystallography is the 'phase problem,' where essential information about crystal phases is missing from diffraction data.
  • This missing phase information hinders the accurate reconstruction of molecular structures.

Purpose of the Study:

  • To address the longstanding phase problem in X-ray crystallography.
  • To highlight recent developments and their impact on resolving phase ambiguities.
  • To discuss advancements in determining crystal phases for small molecules and proteins.

Main Methods:

  • Application of direct methods, including Shake 'n' Bake, SHELXD, CRUNCH, and SIR96, to small molecules and proteins.

Related Experiment Videos

  • Implementation of bias-free refinement using gamma-correction (Solomon).
  • Improvements in phase probability distribution determination (SHARP) and automated atomic refinement (wARP).

    • Main Results:

    • Progress in applying direct methods to small structures, aiding phase determination.
    • Development of bias-free refinement techniques for more accurate structural models.
    • Enhanced methods for calculating phase probability distributions and automated refinement.

    Conclusions:

    • Recent advancements offer improved solutions to the phase problem in X-ray crystallography.
    • These developments facilitate more accurate and efficient structure determination, particularly for small molecules and proteins.
    • The integration of these methods enhances the overall capability of X-ray crystallography.