This book provides a complete introduction to all major topics needed in order to use electron microscopy as a research tool in structural biology. Written by a group of 5 well-known pioneers of the field of electron cryo-microscopy of biological macromolecules, this book offers a depth of knowledge and expertise that could only be replicated from the primary literature with great difficulty.

In the modern world of ever smaller devices and nanotechnology, electron crystallography emerges as the most important method capable of determining the structure of minute objects down to the size of individual atoms. Crystals of only a few millionths of a millimetre are studied. This is the first textbook explaining how this is done. Great attention is given to symmetry in crystals and how it manifests itself in electron microscopy and electron diffraction, and how this symmetry can be determined and taken advantage of in achieving improved electron microscopy images and solving crystal structures from electron diffraction patterns. Theory and practice are combined; experimental images, diffraction patterns, formulae and numerical data are discussed in parallel, giving the reader a complete understanding of what goes on inside the "black boxes" of computer programs. This up-to-date textbook contains the newest techniques in electron crystallography, including detailed descriptions and explanations of the recent remarkable successes in determining the very complex structures of zeolites and intermetallics. The controversial issue of whether there is phase information present in electron micrsocopy images or not is also resolved once and for all. The extensive appendices include computer labs which have been used at various courses at Stockholm University and international schools in electron crystallography, with applications to the textbook. Students can download image processing programs and follow these lab instructions to get a hands-on experience of electron crystallography.

Cryoelectron microscopy of biological molecules is among the hottest growth areas in biophysics and structural biology at present, and Frank is arguably the most distinguished practitioner of this art. CryoEM is likely over the next few years to take over much of the structural approaches currently requiring X-ray crystallography, because one can now get good and finely detailed images of single molecules down to as little as 200,000 MW, covering a substantial share of the molecules of greatest biomedical research interest. This book, the successor to an earlier work published in 1996 with Academic Press, is a natural companion work to our forthcoming book on electron crystallography by Robert Glaeser, with contributions by six others, including Frank. A growing number of workers will employ CryoEM for structural studies in their own research, and a large proportion of biomedical researchers will have a growing interest in understanding what the capabilities and limits of this approach are.

Three-Dimensional Electron Microscopy of Macromolecular Assemblies is the first systematic introduction to single-particle methods of reconstruction. It covers correlation alignment, classification, 3D reconstruction, restoration, and interpretation of the resulting 3D images in macromolecular assemblies. It will be an indispensable resource for newcomers to the field and for all using or adopting these methods.Key Features* Presents methods that offer an alternative to crystallographic techniques for molecules that cannot be crystallized* Describes methods that have been instrumental in exploring the three-dimensional structure of* the nuclear pore complex* the calcium release channel;* the ribosome* chaperonins

Structural Biology Using Electrons and X-Rays discusses the diffraction and image-based methods used for the determination of complex biological macromolecules. The book focuses on the Fourier transform theory, which is a mathematical function that is computed to transform signals between time and frequency domain. Composed of five parts, the book examines the development of nuclear magnetic resonance (NMR), which allows the calculation of the images of a certain protein. Parts 1 to 4 provide the basic information and the applications of Fourier transforms, as well as the different methods used for image processing using X-ray crystallography and the analysis of electron micrographs. Part 5 focuses entirely on the mathematical aspect of Fourier transforms. In addition, the book examines detailed structural analyses of a specimen's symmetry (i.e., crystals, helices, polyhedral viruses and asymmetrical particles). This book is intended for the biologist or biochemist who is interested in different methods and techniques for calculating the images of proteins using nuclear magnetic resonance (NMR). It is also suitable for readers without a background in physical chemistry or mathematics. - Emphasis on common principles underlying all diffraction-based methods - Thorough grounding in theory requires understanding of only simple algebra - Visual representations and explanations of challenging content - Mathematical detail offered in short-course form to parallel the text

This book describes hydration structures of proteins by combining experimental results with theoretical considerations. It is designed to introduce graduate students and researchers to microscopic views of the interactions between water and biological macromolecules and to provide them with an overview of the field. Topics on protein hydration from the past 25 years are examined, most of which involve crystallography, fluorescence measurements, and molecular dynamics simulations. In X-ray crystallography and molecular dynamics simulations, recent advances have accelerated the study of hydration structures over the entire surface of proteins. Experimentally, crystal structure analysis at cryogenic temperatures is advantageous in terms of visualizing the positions of hydration water molecules on the surfaces of proteins in their frozen-hydrated crystals. A set of massive data regarding hydration sites on protein surfaces provides an appropriate basis, enabling us to identify statistically significant trends in geometrical characteristics. Trajectories obtained from molecular dynamics simulations illustrate the motion of water molecules in the vicinity of protein surfaces at sufficiently high spatial and temporal resolution to study the influences of hydration on protein motion. Together with the results and implications of these studies, the physical principles of the measurement and simulation of protein hydration are briefly summarized at an undergraduate level. Further, the author presents recent results from statistical approaches to characterizing hydrogen-bond geometry in local hydration structures of proteins. The book equips readers to better understand the structures and modes of interaction at the interface between water and proteins. Referred to as “hydration structures”, they are the subject of much discussion, as they may help to answer the question of why water is indispensable for life at the molecular and atomic level.

Essentials of Chemical Biology Discover a detailed knowledge of concepts and techniques that shape this unique multi-discipline Chemical Biology is devoted to understanding the way that Biology works at the molecular level. This is a problem-driven multi-discipline, incorporating as it does Organic, Physical, Inorganic, and Analytical Chemistry alongside newer emerging molecular disciplines. In recent years, Chemical Biology has emerged as a vibrant and growing multi-discipline distinct from Biochemistry that is focused on the quantitative analyses of the structures and functions of biological macromolecules and macromolecular lipid assemblies, at first in isolation, then in vitro and in vivo. The second edition of the Essentials of Chemical Biology begins with a thorough introduction to the structure of biological macromolecules and macromolecular lipid assemblies, before moving on to the principles of chemical and biological synthesis, followed by descriptions of a comprehensive variety of research techniques and experimental methods. In addition, the second edition now includes new sections on the behaviour of biological macromolecules and macromolecular lipid assemblies in cells in vitro and in organisms in vivo. Given this, the second edition of the Essentials of Chemical Biology promises to cement itself as the leading introduction to Chemical Biology, incorporating descriptions of cutting-edge research wherever appropriate. Hence, readers of the second edition of the Essentials of Chemical Biology will find: a general expansion in understanding of basic molecular mechanisms in Biology moving towards cellular and organismal mechanisms entirely new chapters covering miniaturization and array technologies, Chemical Cell Biology, and the interface between Chemical Biology and Nanotechnology updates to chapters reflecting recent research developments an increased engagement with medical applications Essentials of Chemical Biology is ideal for advanced undergraduates or (post) graduate students in Chemical Biology and adjacent fields.