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Related Experiment Videos

Crambin: a direct solution for a 400-atom structure.

C M Weeks1, H A Hauptman, G D Smith

  • 1Medical Foundation of Buffalo, NY 14203, USA.

Acta Crystallographica. Section D, Biological Crystallography
|January 1, 1995
PubMed
Summary
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Researchers determined the crystal structure of crambin using an ab initio "shake-and-bake" method. This approach successfully solved the protein structure without anomalous dispersion measurements, achieving high resolution.

Area of Science:

  • Protein crystallography
  • Structural biology
  • Computational methods in structural determination

Background:

  • Crambin's crystal structure was previously solved using anomalous scattering from sulfur atoms.
  • Anomalous dispersion measurements require specific experimental conditions and can be complex.
  • Advancements in computational methods offer alternative approaches to structure determination.

Purpose of the Study:

  • To determine the crystal structure of crambin without relying on anomalous dispersion measurements.
  • To validate the efficacy of the ab initio 'shake-and-bake' method for protein structure solution.
  • To achieve high-resolution structural data for crambin using novel computational techniques.

Main Methods:

  • Application of the ab initio 'shake-and-bake' method.

Related Experiment Videos

  • Phase refinement using minimal function alternated with Fourier refinement.
  • Processing of X-ray diffraction data at 1.1 A resolution.

    • Main Results:

    • Successful determination of the crambin crystal structure without anomalous dispersion.
    • High-resolution (1.1 A) structural data obtained for crambin.
    • Demonstration of the 'shake-and-bake' method's capability for solving protein structures.

    Conclusions:

    • The ab initio 'shake-and-bake' method is a viable alternative to anomalous dispersion for protein crystallography.
    • High-resolution protein structures can be determined computationally.
    • This advancement simplifies and potentially broadens the scope of X-ray crystallography studies.