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Related Experiment Videos

Experience with phase extension and ab initio phase determination in macromolecular crystallography using

L Sjölin1, L A Svensson

  • 1Institute for Inorganic Chemistry, Chalmers University of Technology and University of Göteborg, Sweden.

Acta Crystallographica. Section D, Biological Crystallography
|January 1, 1993
PubMed
Summary

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New maximum-entropy methods successfully determined macromolecular structures, including bovine heart creatine kinase. These tools advance ab initio phase determination and phase extension for complex protein structures.

Area of Science:

  • Crystallography
  • Structural Biology
  • Computational Chemistry

Background:

  • Macromolecular structure determination is crucial for understanding biological function.
  • Ab initio phase determination and phase extension are key challenges in X-ray crystallography.
  • Maximum-entropy methods offer a promising approach to address these challenges.

Purpose of the Study:

  • To develop and test novel maximum-entropy methods for phase extension and ab initio phase determination.
  • To apply these methods to solve previously unknown macromolecular structures.
  • To validate the efficiency and accuracy of the developed tools.

Main Methods:

  • Development of three distinct computational tools based on maximum-entropy principles.
  • Application of a phase expander tool for phase extension.

Related Experiment Videos

  • Utilization of an efficient algorithm for positive electron-density distribution to determine ab initio phases from X-ray diffraction data.

    • Main Results:

    • Successful application of the phase expander tool in solving two unknown macromolecular structures.
    • Determination of X-ray diffraction data phases for recombinant bovine chymosin using maximum-entropy methods.
    • Ab initio phasing of bovine heart creatine kinase structure amplitudes to 2.7 Å resolution.
    • Confirmation of centric reflection phases via Patterson map solution of a mercury derivative.
    • Successful phasing of centric reflections for bovine prothrombin fragment 1 data.

    Conclusions:

    • Maximum-entropy methods provide effective tools for phase extension and ab initio phase determination in crystallography.
    • The developed methods enable the solution of complex macromolecular structures, including proteins with hundreds of residues.
    • These techniques offer a viable alternative to traditional structure solution methods, particularly for challenging datasets.