Macromolecular Crystallography, Part B: Volume 277
Published on 25. September 1997
Book
Hardback
664 pages
978-0-12-182178-4 (ISBN)
Description
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.
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.
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.
Reviews / Votes
Praise for the Series"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
--BIO/TECHNOLOGY
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
--BIO/TECHNOLOGY
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
More details
Series
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
College/higher education
Professional and scholarly
Dimensions
Height: 229 mm
Width: 152 mm
Weight
1080 gr
ISBN-13
978-0-12-182178-4 (9780121821784)
Copyright in bibliographic data is held by Nielsen Book Services Limited or its licensors: all rights reserved.
Schweitzer Classification
Persons
Content
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.
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.