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Related Experiment Videos

Structure determination of turkey egg-white lysozyme using Laue diffraction data.

P L Howell1, S C Almo, M R Parsons

  • 1Chemistry Department, Massachusetts Institute of Technology, Cambridge 02139.

Acta Crystallographica. Section B, Structural Science
|April 1, 1992
PubMed
Summary

The three-dimensional structure of turkey egg-white lysozyme was determined using X-ray crystallography and the Laue method. This study provides insights into protein structure and potential for time-resolved studies.

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Area of Science:

  • Structural Biology
  • X-ray Crystallography
  • Protein Science

Background:

  • Turkey egg-white lysozyme (TEWL) structure determination was re-evaluated due to refinement issues with existing models.
  • Previous attempts to refine the TEWL atomic model (PDB entry 1LZ2) based on C-alpha positions were unsuccessful.

Purpose of the Study:

  • To solve and refine the three-dimensional structure of turkey egg-white lysozyme (TEWL) at 2.5 A resolution.
  • To establish the first protein structure determined using Laue diffraction data.
  • To assess the suitability of this crystal form for time-resolved crystallographic studies.

Main Methods:

  • X-ray diffraction data collection using the Laue method.
  • Molecular replacement using a refined hen egg-white lysozyme model.

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  • Crystallographic refinement employing simulated annealing and least-squares techniques.

    • Main Results:

    • The three-dimensional structure of TEWL was solved and refined to a resolution of 2.5 A.
    • A final residual R factor of 20.7% was achieved.
    • Catalytic residues (Asp52 and Glu35) were found to be solvent-accessible in the crystal structure.

    Conclusions:

    • The refined TEWL structure provides a detailed molecular model.
    • This crystal form is suitable for time-resolved crystallographic studies due to accessible active sites.
    • This work represents a significant advancement in applying Laue diffraction for protein structure determination.