Macromolecular crystallography

著者

• Carter, Charles W.
• Sweet, Robert M.

書誌事項

Macromolecular crystallography

edited by Charles W. Carter, Jr., Robert M. Sweet

（Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 276-277, 368, 374）

Academic Press, c1997-c2003

• pt. A
• pt. B
• pt. C
• pt. D

注記

Pts. C-D: published by Elsevier Academic Press

Includes bibliographical references and indexes

内容説明・目次

巻冊次

pt. A ISBN 9780121821777

内容説明

The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.

目次

Introduction: B.W. Matthews, Recent Transformations in Structural Biology. Crystals: P.C. Weber, Overview of Protein Crystallization Methods. M. Rigs-Kautt and A. Ducruix, Inferences Drawn from Physicochemical Studies of Crystallogenesis and Precrystalline State. L. Song and J.E. Gouaux, Membrane Protein Crystallization: Application of Sparse Matrix to alpha-Hemolysin Heptamer. C.W. Carter, Jr., Response Surface Methods for Optimizing and Improving Reproducibility of Crystal Growth. A. George, Y. Chiang, B. Guo, A. Arabshahi, Z. Cai, and W.W. Wilson, Second Virial Coefficient as Predictor in Protein Crystal Growth. J.R. Luft and G.T. DeTitta, Kinetic Aspects of Macromolecular Crystallization. R. Sousa, Using Cosolvents to Stabilize Protein Conformation for Crystallization. C.E. Kundrot, Preparation and Crystallization of RNA: A Sparse Matrix Approach. A.R. Ferre-Damare and S.K. Burley, Dynamic Light Scattering in Evaluating Crystallizability of Macromolecules. A.M. Edwards, S.A. Darst, S.A. Hemming, F.J. Asturias, P.R. David, and R.D. Kornberg, Two-Dimensional Protein Crystals in Aid of Three-Dimensional Protein Crystal Growth. I. Rayment, Reductive Alkylation of Lysine Residues to Alter Crystallization Properties of Proteins. Data: Cryocrystallography: D. Rodgers, Practical Cryocrystallography. J.R. Helliwell, Overview of Synchrotron Radiation and Macromolecular Crystallography. Z.R. Korszun, Neutron Macromolecular Crystallography. Detectors:Y. Amemiya, X-Ray Storage-Phosphor Imaging-Plate Detectors: High-Sensitivity X-Ray Area Detector. E.M. Westbrook and I. Naday, Charge-Coupled Device-Based Area Detectors. R. Kahn and R. Fourme, Gas Proportional Detectors. Data Collection Software:J.W. Pflugrath, Diffraction-Data Processing for Electronic Detectors: Theory and Practice. Z. Otwinowski and W. Minor, Processing of X-Ray Diffraction Data Collected in Oscillation Mode. Z. Dauter, Data Collection Strategy. T.O. Yeates, Detecting and Overcoming Crystal Twinning. Phases: Basic Concepts:G. Bricogne, Bayesian Statistical Viewpoint on Structure Determination: Basic Concepts and Examples. G. Bricogne, Efficient Sampling Methods for Combinations of Signs, Phases, Hyperphases, and Molecular Orientations. H. Ke, Overview of Isomorphous Replacement Phasing. M.A. Rould, Screening for Heavy-Atom Derivatives and Obtaining Accurate Isomorphous Differences. E. de La Fortelle and G. Bricogne, Maximum-Likelihood Heavy-Atom Parameter Refinement for Multiple Isomorphous Replacement and Multiwavelength Anomalous Diffraction Methods. Multiwavelength Methods:W.A. Hendrickson and C.M. Ogata, Phase Determination by Multiwavelength Anomalous Diffraction Methods. S. Doublie, Preparation of Selenomethionyl Proteins for Phase Determination. T.C. Terwilliger, Multiwavelength Anomalous Diffraction Phasing of Macromolecular Structures: Analysis of MAD Data as Single Isomorphous Replacement with Anomalous Scattering Data Using MADMRG Program. V. Ramakrishnan and V. Biou, Treatment of Multiwavelength Anomalous Diffraction Data as a Special Case of Multiple Isomorphous Replacement. Molecular Replacement:A.T. Branger, Patterson Correlation Searches and Refinement. J. Navaza and P. Saludjian, AMoRe: An Automated Molecular Replacement Program Package. L. Tong and M. Rossmann, Rotation Function Calculations with GLRF Program. G.A. Bentley, Phased Translation Function. Horizon MethodsJ.M. Berg and N.W. Goffeney Centrosymmetric Crystals of Biomolecules: The Racemate Method. G.M. Sheldrick, Patterson Superposition and ab Initio Phasing. A.D. Podjarny and A.G. Urzhumtsev, Low-Resolution Phasing. Author Index. Subject Index.

巻冊次

pt. B ISBN 9780121821784

内容説明

Macromolecular Crystallography, Part B is the"linch-pin"of the ongoing revolution in structural biology. In the past decade, fundamental transformations of nearly every technical aspect of structure determination by X-ray diffraction have taken place. The contributions of this volume and its companion Volume 276 emphasize the revision and extension of statistical tools that underly all phases of structure determination, the practical and conceptual impact of synchrotron radiation, horizon phase-determination methods, and computerized automation.

目次

Phases: Horizon Methods: H.A. Hauptman, Shake and Bake: An Algorithm for Automatic Solution ab Initio of Crystal Structures. G. Bricogne, Ab Initio Macromolecular Phasing: A Blueprint for an Expert System Based on Structure Factor Statistics with Built-In Stereochemistry. Model-Independent Map Refinement: F.M.D. Vellieux and R.J. Read, Noncrystallographic Symmetry Averaging in Phase Refinement and Extension. K.Y.J. Zhang, K. Cowtan, and P. Main, Combining Constraints for Electron Density Modification. C.J. Gilmore and G. Bricogne, MICE Computer Program. C.W. Carter and S. Xiany, Phase Improvement Using Conditional Probability Methods: Maximum Entropy Solvent Flattening with Phase Permutation. R.J. Read, Model Phases: Probabilities and Bias. Models: Model Building: S. Fortier, A. Chiverton, J. Glasgow, and L. Leherte, Critical-Point Analysis in Protein Electron-Density Map Interpretation. J.S.Sack and F.A. Quiocho, Chain: A Crystallographic Modeling Program. T.A. Jones and M. Kjeldgaard, Electron Density Map Interpretation. G.J. Kleywegt and T.A. Jones, Model Building and Refinement Practice. B.C. Finsel, LORE: Exploiting Database of Known Structures. Refinement: A.T. Branger and L.M. Rice, Crystallographic Refinement by Simulated Annealing: Methods and Applications. V.S. Lamzin and K.S. Wilson, Automated Refinement for Protein Crystallography. D.E. Tronrud, The TNT Refinement Package. G.M. Sheldrick and T.R. Schneider, SHELXL: High-Resolution Refinement. J. Badger and D.L. Caspar, Modeling and Refinement of Water Molecules and Disordered Solvent. L.H. Jensen, Refinement and Reliability of Macromolecular Models Based on X-Ray Diffraction Data. Verification: Safe Crystallography: A. T. Branger, Free R Value: A More Objective Statistic for Crystallography. D. Eisenberg, R. Lathy, and J.U. Bowie, VERIFY3D: Assessment of Protein Models with Three-Dimensional Profiles. Dynamic Properties: From Static Diffraction Data: J.B. Clarage and G.N. Phillips, Jr., Analysis of Diffuse Scattering and Relation to Molecular Motion. From Time-Resolved Studies: Laue Diffraction: K. Moffat, Laue Diffraction. I.J. Clifton, E.M.H. Duke, S. Wakatsuki, and Z. Ren, Evaluation of Laue Diffraction Diagrams. I. Schlichting and R.S. Goody, Triggering Methods in Crystallographic Enzyme Kinetics. Presentation and Analysis: Illustrating Structures: M. Carson, Ribbons. E.A. Merrit and D.J. Bacon, Raster3D: Photorealistic Molecular Graphics. Modeling Structures: G.J. Kleywegt and T.A. Jones, Detecting Folding Motifs and Similarities in Protein Structures. Databases: G.L. Gilliland, Biological Macromolecule Crystallization Database. E.E. Abola, J.L. Sussman, J. Prilusky, and N.O. Manning, Protein Data Bank Archives of Three-Dimensional Macromolecular Structures. P.E. Bourne, H.M. Berman, J.D. Westbrook, B. McMahon, K.D. Watenpaugh, and P.M.D. Fitzgerald, Macromolecular Crystallographic Information File. Program Packages: W.F. Furey and S. Swaminathan, Phases-95: A Program Package forProcessing and Analyzing Diffraction Data from Macromolecules. M. Winn, E.J. Dodson, and A. Ralph, Collaborative Computational Project, Number 4: Providing Programs for Protein Crystallography. Author Index. Subject Index.

巻冊次

pt. C ISBN 9780121822712

内容説明

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.

巻冊次

pt. D ISBN 9780121827779

内容説明

Accurate molecular structures is 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.

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詳細情報

• NII書誌ID(NCID): BA29765353
• ISBN:
  • 0121821773
  • 0121821781
  • 0121822710
  • 0121827771
• 出版国コード: us
• タイトル言語コード: eng
• 本文言語コード: eng
• 出版地: San Diego ; Tokyo
• ページ数/冊数: 4 v.
• 大きさ: 24 cm
• 親書誌ID:
  • BA00197543