Macromolecular Crystallography, Part B, Volume 277 (Methods in Enzymology)

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 andRefinement 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.

Audience: Biochemists, biophysicists, analytical chemists, and physical chemists.