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.
Clear, concise explanation of logical development of basic crystallographic concepts. Topics include crystals and lattices, symmetry, x-ray diffraction, and more. Problems, with answers. 114 illustrations. 1969 edition.
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.
Structural Glycobiology covers the experimental, theoretical, and alternative technologies used in the study of the structural basis for the diverse biological roles of carbohydrates. The book overviews the application of specialized technologies to the study of carbohydrates in biology, reviews relevant and current research in the field, and is illustrated throughout by specific examples of how research investigations have yielded key structural and associated biological data on carbohydrates and glycolipids. In particular, the book focuses on: X-ray crystallography and small-angle scattering, NMR, and cryo-electron microscopy techniques Theoretical (modeling-based) approaches, such as molecular mechanics, molecular dynamics, free energy calculations, and carbohydrate docking Alternative techniques for yielding structural information on carbohydrates from complex biological samples Carbohydrates in medicine, specifically in areas that have been directly impacted by our understanding of the structural role of carbohydrates in immune recognition: cancer, organ transplantation, and infection
Crystal Structure Refinement is a mixture of textbook and tutorial. As A Crystallographers Guide to SHELXL it covers advanced aspects of practical crystal structure refinement, which have not been much addressed by textbooks so far. After an introduction to SHELXL in the first chapter, a brief survey of crystal structure refinement is provided. Chapters three and higher address the various aspects of structure refinement, from the treatment of hydrogen atoms to the assignment of atom types, to disorder, to non-crystallographic symmetry and twinning. One chapter is dedicated to the refinement of macromolecular structures and two short chapters deal with structure validation (one for small molecule structures and one for macromolecules). In each of the chapters the book gives refinement examples, based on the program SHELXL, describing every problem in detail. It comes with a CD-ROM with all files necessary to reproduce the refinements.
X-ray crystallography is the main method used to determine the structure of biological molecules. X-ray crystallography is explained without maths and reading this text allows biologists to assess the quality and accuracy of biological structures.
The binding of small ligands to biological molecules is central to most aspects of biological function. The past twenty years has seen the development of an increasing armoury of biophysical methods that not only detect such binding, but also provide varying degrees of information about the kinetics, thermodynamics and structural aspects of the process. These methods have received increasing attention with the growth in more rational approaches to drug discovery and design. This book reviews the latest advances in the application of biophysics to the study of ligand binding. It provides a complete overview of current techniques to identify ligands, characterise their binding sites and understand their binding mechanisms. Particular emphasis is given to the combined use of different techniques and their relative strengths and weaknesses. Consistency in the way each technique is described makes it easy for readers to select the most suitable protocol for their research. The introduction explains why some techniques are more suitable than others and emphasizes the possible synergies between them. The following chapters, all written by a specialist in the particular technique, focus on each method individually. The book finishes by describing how several complimentary techniques can be used together for maximum effectiveness. This book is suitable for biomolecular scientists at graduate or post-doctoral level in academia and industry. Biologists and chemists will also find it a useful introduction to the techniques available.
