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Crystals, x-rays, and proteins: comprehensive protein crystallography/ Dennis Sherwood and Jon Cooper.

By: Contributor(s): Publication details: Oxford: Oxford University Press, 2015.Description: xvii, 625 p. illustrationsISBN:
  • 9780198726326 (Pbk.)
Subject(s): DDC classification:
  • 548.83 Q5
Online resources:
Contents:
Machine generated contents note: -- 1. The crystalline state and its study -- 2. Vector analysis and complex algebra -- 3. Crystal systematics -- 4. Waves and electromagnetic radiation -- 5. Fourier transforms and convolutions -- 6. Diffraction --7. Diffraction from one-dimensional obstacles -- 8. Diffraction from a three-dimensional lattice -- 9. The contents of the unit cell -- 10. Experimental methods : sample preparation -- 11. Experimental techniques : data collection and analysis -- 12. The phase problem and the Patterson function --13. Molecular replacement -- 14. Solving the phase problem experimentally -- 15. Model building and refinement -- 16. Complementary crystallographic methods.
Summary: "A complete account of the theory of the diffraction of x-rays by crystals with particular reference to the processes of determining the structures of protein molecules, this book is aimed primarily at structural biologists and biochemists but will also be valuable to those entering the field with a background in physical sciences or chemistry. It may be used at any post-school level, and develops from first principles all relevant mathematics, diffraction and wave theory, assuming no mathematical knowledge beyond integral calculus. The book covers a host of important topics in the area, including:- The practical aspects of sample preparation and x-ray data collection, using both laboratory and synchrotron sources - Data analysis at both theoretical and practical levels- The important role played by the Patterson function in structure analysis by both molecular replacement and experimental phasing approaches - Methods for improving the resulting electron density map - The theoretical basis of methods used in refinement of protein crystal structures - In-depth explanation of the crucial task of defining the binding sites of ligands and drug molecules - The complementary roles of other diffraction methods which reveal further detail of great functional importance in a crystal structure"--
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Holdings
Item type Current library Call number Status Date due Barcode Item holds
Books Books Mahatma Gandhi University Library General Stacks 548.83 Q5 (Browse shelf(Opens below)) Available 54274
Total holds: 0

Includes bibliographical references (pages 616-620) and index.

Machine generated contents note: -- 1. The crystalline state and its study -- 2. Vector analysis and complex algebra -- 3. Crystal systematics -- 4. Waves and electromagnetic radiation -- 5. Fourier transforms and convolutions -- 6. Diffraction --7. Diffraction from one-dimensional obstacles -- 8. Diffraction from a three-dimensional lattice -- 9. The contents of the unit cell -- 10. Experimental methods : sample preparation -- 11. Experimental techniques : data collection and analysis -- 12. The phase problem and the Patterson function --13. Molecular replacement -- 14. Solving the phase problem experimentally -- 15. Model building and refinement -- 16. Complementary crystallographic methods.

"A complete account of the theory of the diffraction of x-rays by crystals with particular reference to the processes of determining the structures of protein molecules, this book is aimed primarily at structural biologists and biochemists but will also be valuable to those entering the field with a background in physical sciences or chemistry. It may be used at any post-school level, and develops from first principles all relevant mathematics, diffraction and wave theory, assuming no mathematical knowledge beyond integral calculus. The book covers a host of important topics in the area, including:- The practical aspects of sample preparation and x-ray data collection, using both laboratory and synchrotron sources - Data analysis at both theoretical and practical levels- The important role played by the Patterson function in structure analysis by both molecular replacement and experimental phasing approaches - Methods for improving the resulting electron density map - The theoretical basis of methods used in refinement of protein crystal structures - In-depth explanation of the crucial task of defining the binding sites of ligands and drug molecules - The complementary roles of other diffraction methods which reveal further detail of great functional importance in a crystal structure"--

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