Synthesizing over thirty years of advances into a comprehensive textbook, Biomolecular Crystallography describes the fundamentals, practices, and applications of protein crystallography. Illustrated in full-color by the author, the text describes mathematical and physical concepts in accessible and accurate language. Biomolecular Crystallography will be a valuable resource for advanced undergraduate and graduate students and practitioners in structural biology, crystallography, and structural bioinformatics.

This work presents a snapshot of the state of the art of modern biomolecular crystallography, from crystallisation through structure determination and even interactive presentation on the web. Methods driving the latest automated structure determination pipelines are explained, as well as how to deal with problems such as crystal pathologies that still demand expert analysis. These methods are illustrated through their application to problems of great biological interest, such as the molecular machinery underlying the complement pathway, the mechanism of action of monoamine oxidase inhibitors, and the structure of the eukaryotic ribosome. Complementary approaches, such as neutron diffraction, small angle X-ray scattering, coherent diffraction and computational modelling, are also explored.

Crystallography Made Crystal Clear is designed to meet the need for an X-ray analysis that is between brief textbook sections and complete treatments. The book provides non-crystallographers with an intellectually satisfying explanation of the principles of how protein models are gleaned from X-ray analysis. The understanding of these concepts will foster wise use of the models, including the recognition of the strengths and weaknesses of pictures or computer graphics. Since proteins comprise the majority of the mass of macromolecules in cells and carry out biologically important tasks, the book will be of interest to biologists.Provides accessible descriptions of principles of x-ray crystallography, built on simple foundations for anyone with a basic science backgroundLeads the reader through clear, thorough, unintimidating explanations of the mathematics behind crystallographyExplains how to read crystallography papers in research journalsIf you use computer-generated models of proteins or nucleic acids for:Studying molecular interactionsDesigning ligands, inhibitors, or drugsEngineering new protein functionsInterpreting chemical, kinetic, thermodynamic, or spectroscopic dataStudying protein foldingTeaching macromolecule structure,and if you want to read new structure papers intelligently; become a wiser user of macromolecular models; and want to introduce undergraduates to the important subject of x-ray crystallography, then this book is for you.

The proteome remains a mysterious realm. Researchers have determined the structures of only a small fraction of the proteins encoded by the human genome. Crystallography continues to be the primary method used to determine the structures of the remaining unknown proteins. This imaging technique uses the diffraction of X-rays to determine a protein’s three-dimensional molecular structure. Drawing on years of research and teaching experience, Eaton E. Lattman and Patrick J. Loll use clear examples and abundant illustrations to provide a concise and accessible primer on protein crystallography. Discussing the basics of diffraction, the behavior of two- and three-dimensional crystals, phase determination (including MIR and MAD phasing and molecular replacement), the Patterson function, and refinement, Lattman and Loll provide a complete overview of this important technique, illuminated by physical insights. The crisp writing style and simple illustrations will provide beginner crystallographers with a guide to the process of unraveling protein structure.

This volume is a collection of the contributions presented at the 42nd Erice Crystallographic Course whose main objective was to train the younger generation on advanced methods and techniques for examining structural and dynamic aspects of biological macromolecules. The papers review the techniques used to study protein assemblies and their dynamics, including X-ray diffraction and scattering, electron cryo-electron microscopy, electro nanospray mass spectrometry, NMR, protein docking and molecular dynamics. A key theme throughout the book is the dependence of modern structural science on multiple experimental and computational techniques, and it is the development of these techniques and their integration that will take us forward in the future.

The rational, structure-based approach has become standard in present-day drug design. As a consequence, the availability of high-resolution structures of target proteins is more often than not the basis for an entire drug development program. Protein structures suited for rational drug design are almost exclusively derived from crystallographic studies, and drug developers are relying heavily on the power of this method. Here, researchers from leading pharmaceutical companies present valuable first-hand information, much of it published for the first time. They discuss strategies to derive high-resolution structures for such important target protein classes as kinases or proteases, as well as selected examples of successful protein crystallographic studies. A special section on recent methodological developments, such as for high-throughput crystallography and microcrystallization, is also included. A valuable companion for crystallographers involved in protein structure determination as well as drug developers pursuing the structure-based approach for use in their daily work.

X-ray crystallography provides a unique opportunity to study the arrangement of atoms in a molecule. This book's modern computer-graphics centered approach facilitates the extrapolation of these valuable observations. A unified treatment of crystal systems, the book explains how atoms are arranged in crystals using the metric matrix. Featuring t