Elementary X-Ray Diffraction for Biologists

Jenny P. Glusker

The Institute for Cancer Research, The Fox Chase Cancer Centre, Philadelphia, PA 19111

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• 1. General Teaching
  • a. 10 minute talk
  • b. Course of 4 hours (usually with lots of solicited student interruptions)
• 2. Some Textbooks
• 3. Molecular Dimensions
  • a. Bond lengths and angles
  • b. Torsion angles
  • c. Molecular packing
  • d. Stereoviews
• 4. Absolute Configuration
  • a. R/S system
  • b. Fischer formulae
  • c. Newman projection
  • d. Example. (+)-hydroxycitric acid
• 5. The Resolution of the Structure
• 6. Differences in Techniques for Small and Large Molecules
• 7. Small Structures in Biology
  • a. Uses of cell dimensions and refractive indices
  • b. Determination of chemical formulae
  • c. Studies of flexible molecules to obtain comformational information
  • d. Studies of molecular packing and hydrogen bonding
  • e. Studies of enzyme mechanism utilizing structures of substrates and inhibitors
  • f. Comparisons of structures using the Cambridge Crystallographic Data file
• 8. Enzymes and Other Proteins
  • Lysozyme
  • Ribonuclease
  • Carboxypeptidase A
  • Hemoglobin
  • Chymotrypsin
  • Alcohol dehydrogenase
• 9. Immunochemistry
• 10. Membranes
• 11. Nucleic Acids
  • Biology of DNA
  • Transfer RNA
• 12. Structures of Viruses
• Acknowledgement

Teaching Aims

To teach about some of the basic structural results obtained by X-ray diffraction studies, and their relevance, to biochemistry and biology undergraduate-level students and beyond.

Background Required

None.

Practical Resources

Time Required for Teaching

This could be incorporated as one or two lectures in a general course on biophysical methods or it could form the basis for a complete course on protein and nucleic acid structure.

Copyright © 1984, 1997 International Union of Crystallography