Macromolecular crystallography. Part C [electronic resource] / edited by Charles W. Carter, Jr., Robert M. Sweet.

Contributor(s): Carter, Charles W | Sweet, Robert MMaterial type: Text

TextSeries: Methods in enzymology ; v. 368.Publication details: Amsterdam ; Oxford : Elsevier Academic Press, �2003. Description: 1 online resource (xxxii, 368 pages, [4] pages of plates) : illustrations (some color)Content type: text Media type: computer Carrier type: online resourceISBN: 0080497098 (electronic bk.); 9780080497099 (electronic bk.); 0121822710 (electronic bk.); 9780121822712 (electronic bk.)Subject(s): X-ray crystallography | Enzymes -- Analysis | Proteins -- Analysis | Enzymes -- Analysis | Proteins -- Analysis | X-ray crystallographyGenre/Form: Electronic books.DDC classification: 548.3 LOC classification: QP601Online resources: ScienceDirect | ScienceDirect

Contents:

Cover -- Table of Contents -- Contributor to Volume 368 -- Preface -- Volumes in Series -- Section I: Reminiscences on Methods -- Chapter 1. Transformations in Structural Biology: Personal View -- Chapter 2. Origins -- Chapter 3. Personal X-ray Reflections -- Section II: Crystals -- Chapter 4. Robotics for Automated Crystal Formation and Analysis -- Chapter 5. Use of Limited Proteolysis to Identify Protein Domains Suitable for Structural Analysis -- Chapter 6. Solvent Entropy Effects in the Formation of Protein Solid Phases -- Chapter 7. Controlling Biomolecular Crystallization by Understanding the Distinct Effects of PEGs and Salts on Solubility -- Chapter 8. Counter-diffusion Methods for Macromolecular Crystallization -- Chapter 9. Growth Sectors and Crystal Quality -- Chapter 10. Molecular Mechanisms of Defect Formation -- Chapter 11. Cryocooling of Macromolecular Crystals: Optimization Methods -- Chapter 12. The Well-Tempered Protein Crystal:Annealing Macromolecular Crystals -- Section III: Data -- Chapter 13. What Can I Have As a Source of X-Ray Synchrotron Radiation? A Primer for Potential Users -- Chapter 14. Protein Crystal Structure Analysis from High- Resolution X-Ray Powder-Diffraction Data -- Chapter 15. Macromolecular Crystal Quality -- Chapter 16. Protein Structures at Atomic Resolution -- Author Index -- Subject Index -- Color Plates Section -- Last Page.

Summary: Accurate molecular structures are vital for rational drug design and for structure-based functional studies directed toward the development of effective therapeutic agents and drugs. Crystallography can reliably predict structure, both in terms of folding and atomic details of bonding. * Methodological methods in crystals * Methodological methods data analysis.

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Includes bibliographical references and index.

Accurate molecular structures are vital for rational drug design and for structure-based functional studies directed toward the development of effective therapeutic agents and drugs. Crystallography can reliably predict structure, both in terms of folding and atomic details of bonding. * Methodological methods in crystals * Methodological methods data analysis.

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