Protein Crystallography

Eaton E. Lattman is chair of the Department of Biophysics at the Johns Hopkins University and editor-in-chief of the journal Proteins: Structure, Function, and Genetics. Patrick J. Loll is the director of the Biochemistry Graduate Program at Drexel University College of Medicine.

Preface
1. Introduction
1.1. What Is X-ray Crystallography?
1.2. A Quick Look at Protein Crystals
1.3. Noncrystalline Specimens
1.4. Summary
Further Reading
2. A Physical Understanding of Diffraction
2.1. What Is Diffraction?
2.2. Diffraction from One-Dimensional Crystals
2.3. Reconstructing Images from Diffraction Patterns
2.4. Summary
Further Reading
3. Diffraction from Three-Dimensional Crystals
3.1. The Electron Density Function in Three Dimensions
3.2. Calculating the Diffraction Pattern from a Known Structure
3.3. Summary
Further Reading
4. Phase Determination by Isomorphous Replacement
4.1. Measuring the Phases
4.2. MAD Phasing
4.3. Fitting Models to Experimental Electron Density Maps
4.4. Summary
Further Reading
5. The Patterson Function
5.1. Definition of the Patterson Function
5.2. Using the Patterson Function to Locate Atoms
5.3. Summary
Further Reading
6. Phasing with Partially Known Structures
6.1. Difference Fourier Maps
6.2. Molecular Replacement
6.3. Summary
Further Reading
7. Crystallographic Refinement
7.1. Refinement Improves the Model
7.2. Least-Squares Refinement
7.3. Summary
Further Reading
Glossary
Index