Macromolecular crystallization and crystal perfection /
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| Author / Creator: | Chayen, Naomi E. |
|---|---|
| Imprint: | Oxford ; New York : Oxford University Press, 2010. |
| Description: | x, 221 p. : ill. ; 25 cm. |
| Language: | English |
| Series: | IUCr monographs on crystallography ; 24 International Union of Crystallography monographs on crystallography ; 24. |
| Subject: | |
| Format: | E-Resource Print Book |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/8138844 |
Table of Contents:
- Preface
- Acknowledgements
- Part I. Introduction and Overview
- 1. Introduction
- 1.1. Crystal growth
- 1.2. Diffraction techniques
- 1.2.1. X-rays
- 1.2.2. Neutrons
- 1.3. Crystal volume and quality
- 1.3.1. Short-range order (intermolecular)
- 1.3.2. Long-range order (domain structure)
- 1.3.3. The combination of short- and long-range order
- 1.4. Chapter summary
- Part II. Crystallization
- 2. Crystallization theory
- 2.1. Chapter summary
- 3. Practical methods of crystallization
- 3.1. Batch
- 3.2. Vapour diffusion
- 3.3. Dialysis
- 3.4. Free interface diffusion
- 3.5. Converting between methods
- 3.6. Chapter summary
- 4. Screening
- 4.1. Screens: problems and new developments
- 4.2. Automation-and miniaturization of screening procedures
- 4.2.1. The effect of high-throughput: crystallization robotics
- 4.2.2. Analysis of large quantities of crystallization data
- 4.2.3. Experiment volume considerations
- 4.2.4. Imaging and monitoring of crystallization trials
- 4.3. Chapter summary
- 5. Optimization
- 5.1. Practical uses of the crystallization phase diagram
- 5.2. Methods for separating nucleation and growth
- 5.2.1. Seeding
- 5.2.2. Dilution techniques
- 5.3. The application o flight-scattering techniques
- 5.3.1. Static light scattering
- 5.3.2. Dynamic light scattering
- 5.4. Chapter summary
- 6. Strategies to apply when high-quality crystals cannot be obtained
- 6.1. Introduction
- 6.2. Non-covalent modification of the sample
- 6.3. Covalent modification of the sample
- 6.3.1. Reductive methylation
- 6.3.2. General chemical modification
- 6.4. Mutagenesis, domain refinement and homologues
- 6.4.1. Surface-entropy reduction
- 6.4.2. Proteolysis
- 6.4.3. Orthologues and homologues
- 6.5. Antibody fragments
- 6.6. Chapter summary
- 7. Membrane proteins
- 7.1. Introduction
- 7.2. Crystallization
- 7.2.1. Screening with detergents
- 1.2.2. Lipidic cubic-phase crystallization
- 7.2.3. Antibody fragment approaches
- 7.3. Characterization using neutron-enhanced contrast
- 7.4. Chapter summary
- 8. Alternative approaches
- 8.1. Gel growth
- 8.2. Microgravity
- 8.2.1. Interferometry
- 8.2.2. Depletion zone
- 8.3. Microfluidics
- 8.4. Magnetic and electric fields
- 8.5. Chapter summary
- Part III. Diffraction
- 9. Experimental aspects
- 9.1. The diffraction pattern
- 9.2. Structural detail
- 9.3. Determining structure when the resolution is not ideal
- 9.4. How accurate is the structure?
- 9.5. Chapter summary
- 10. Analysis of the molecular short-range order
- 10.1. Structural data
- 10.2. Thermal motion and diffuse scattering
- 10.2.1. Diffuse scattering as a source of measurement error in the Bragg intensities
- 10.3. Chapter summary
- 11. Analysis of long-range order
- 11.1. Reflection profiling
- 11.2. Topography
- 11.2.1. Photography-based topography
- 11.2.2. Digital-based topography
- 11.3. Reciprocal-space mapping
- 11.4. Combinational analysis and chapter summary
- 12. Macromolecular crystals and twinning
- 12.1. Historical examples
- 12.2. Types of twinning
- 12.3. The twin fraction and testing for twinned data
- 12.4. Using twinned data
- 12.5. Overcoming twinning in crystals
- 12.6. How prevalent is twinning?
- 12.7. Chapter summary
- 13. Other macromolecular crystal diffraction disorders
- 13.1. Introduction
- 13.2. Case studies
- 13.3. Chapter summary
- 14. Degradation and improvement of crystal perfection
- 14.1. Ageing
- 14.2. Radiation damage
- 14.3. Cryo-cooling
- 14.4. Dehydration and humidity control
- 14.5. Chapter summary
- 15. Unusual diffraction geometries
- 15.1. Chapter summary
- 16. Making the most of difficult crystals - beamline and detector optimization
- 16.1. Introduction
- 16.2. Geometry and end-station instrumentation
- 16.3. Signal and noise considerations
- 16.4. Very small crystal volume'microcrystals'
- 16.5. Phasing and the available instrumentation
- 16.6. Robotics, telepresence and remote access
- 16.7. More specialized applications
- 16.8. Chapter summary
- 17. Protein powders-making the most of tiny crystallites in bulk
- 17.1. Introduction
- 17.2. Quantitative protein powder analyses have opened up in recent years
- 17.3. Structure determination of unknown proteins?
- 17.4. Characterization of protein crystal polymorphism
- 17.5. Chapter summary
- 18. Complementary techniques
- 18.1. Chapter summary
- Part IV. The Future
- 19. The X-ray laser and the single molecule - no crystal needed?
- 20. Overall summary and future thoughts
- Glossary of abbreviations, terms and symbols
- Abbreviations
- General
- Synchrotron sources
- Neutron sources
- Terms
- Crystallization
- X-ray analysis
- Symbols
- Crystallization and crystal-growth-monitoring symbols
- Diffraction symbols
- References
- Index
