X-Ray Crystallography of Biomacromolecules A

Written by one of the most significant contributors to the progress of protein crystallography, this practical guide contains case studies, a troubleshooting section and pointers on data interpretation. It covers the theory, practice and latest achievements in x-ray crystallography, such that any researcher in structural biology will benefit from this extremely clearly written book.Part A covers the theoretical basis and such experimental techniques as principles of x-ray diffraction, solutions for the phase problem and time-resolved x-ray crystallography. Part B includes case studies for different kinds of x-ray crystal structure determination, such as the MIRAS and MAD techniques, molecular replacement, and the difference Fourier technique.

Professor Dr. Albrecht Messerschmidt is group leader at the Max Planck Institute for Biochemistry, Marinsried, Germany.
His main reserach interest is in the determination of X-ray structures of metalloproteins and -enzymes, PLP-dependent enzymes, CoA-transferases and other proteins. His group is part of the department of X-ray structure determination of proteins headed by nobel laureate Robert Huber.

Ptreface
Principles and Methods
Introduction
Crystals and Symmetry
Protein Solubility
Experimental Techniques
Crystallization Screenings
High-Throughput Crystallization, Imaging, and Analysis. References
Experimental Techniques
X-Ray Sources
Detectors
Crystal Mounting and Cooling
Data Collection Techniques. References
Principles of X-Ray Diffraction by a Crystal
Rational Mathematical Representation of Waves
Principles of X-Ray Diffraction by a Crystal. References
Diffraction Data Evaluation
Introductory Remarks
Geometric Principles in the Rotation Technique with Normal Flat Detector
Autoindexing of Oscillation Images
Beam Divergence, Mosaicity, and Partiality
Integration of Diffraction Spots
Post-Refinement, Scaling, and Averaging of Diffraction Data. References
Methods for Solving the Phase Problem
Isomorphous Replacement
Anomalous Scattering
Determination of Heavy-Atom Positions
Phase Calculation
Patterson Search Methods (Molecular Replacement). References
Phase Improvement by Density Modification and Phase Combination
Introduction
Solvent Flattening
Histogram Matching
Molecular Averaging
Sayre's Equation
Atomization
Phase Combination
Difference Fourier Technique. References
Model Building and Refinement
Model Building
Crystallographic Refinement
Verification and Accuracy of Structure Determination. References
Crystal Structure Determination of the Time-Course of Reactions and of Unstable Species
Introduction
Triggering Methods
Trapping Methods
Laue Diffraction. References
Structural Genomics
Introduction
Target Selection
Production of Recombinant Proteins
Aspects of Automation. References
Practical Examples. Introductory Remarks
Data Evaluation
Autoindexing, Refinement of Cell Parameters, and Reflection Integration
Scaling of Intensity Diffraction Data
A Complex Example of Space Group Determination. References
Determination of Anomalous Scatterer or Heavy Atom Positions
Application of Direct Methods
Vector Verification Methods
Comparison of the Results from SnB and RSPS. References
MIRAS and MAD Phasing with the Program SHARP
MAD Phasing with the Program SHARP for 4-BUDH. References
Molecular Replacement
Phase Determination of PKC-iota with Program Molrep. References
Averaging about Non-Crystallographic Symmetry (NCS) for 4-BUDH
Determination of NCS Operators for 4-BUDH
Electron Density Map Averaging for 4-BUDH. References
Model Building and More
A Very Personal Short Introduction to the Computer Graphics Modeling Program "O"
Introduction of the Four Fe-Sites per Fe-S-Cluster and New SHARP-Phasing for 4-BUDH
Crystallographic Refinement and Final Steps
References
Subject Index
Table of Contents provided by Publisher. All Rights Reserved.

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X-Ray Crystallography of Biomacromolecules A Practical Guide

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