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.

With the most comprehensive and up-to-date overview of structure-based drug discovery covering both experimental and computational approaches, Structural Biology in Drug Discovery: Methods, Techniques, and Practices describes principles, methods, applications, and emerging paradigms of structural biology as a tool for more efficient drug development. Coverage includes successful examples, academic and industry insights, novel concepts, and advances in a rapidly evolving field. The combined chapters, by authors writing from the frontlines of structural biology and drug discovery, give readers a valuable reference and resource that: Presents the benefits, limitations, and potentiality of major techniques in the field such as X-ray crystallography, NMR, neutron crystallography, cryo-EM, mass spectrometry and other biophysical techniques, and computational structural biology Includes detailed chapters on druggability, allostery, complementary use of thermodynamic and kinetic information, and powerful approaches such as structural chemogenomics and fragment-based drug design Emphasizes the need for the in-depth biophysical characterization of protein targets as well as of therapeutic proteins, and for a thorough quality assessment of experimental structures Illustrates advances in the field of established therapeutic targets like kinases, serine proteinases, GPCRs, and epigenetic proteins, and of more challenging ones like protein-protein interactions and intrinsically disordered proteins

This book provides a complete snapshot of various experimental approaches to structure-based and ligand-based drug design and is illustrated with more than 200 images.

Crystals have fascinated us for centuries with their beauty and symmetry, and have often been invested with magical powers. The use of X-ray diffraction, first pioneered in 1912 by father and son William and Lawrence Bragg, enabled us to probe the structure of molecules, and heralded the scientific study of crystals, leading to an understanding of their atomic arrangements at a fundamental level. The new discipline, called X-ray crystallography, has subsequently evolved into a formidable science that underpins many other scientific areas. Starting from the determination of the structures of very simple crystals, such as that of common salt, today it has become almost routine to determine the positions of tens of thousands of atoms in a crystal. In this Very Short Introduction Mike Glazer shows how the discoveries in crystallography have been applied to the creation of new and important materials, to drugs and pharmaceuticals and to our understanding of genetics, cell biology, proteins, and viruses. Tracing the history of crystallography, he analyses astonishing developments in new sources of X-rays, as well as of neutrons, and in electron microscopy, and considers the impact they have on the study of crystals today. ABOUT THE SERIES: The Very Short Introductions series from Oxford University Press contains hundreds of titles in almost every subject area. These pocket-sized books are the perfect way to get ahead in a new subject quickly. Our expert authors combine facts, analysis, perspective, new ideas, and enthusiasm to make interesting and challenging topics highly readable.

A textbook for the student beginning a serious study of X-ray crystallography.

Present at the Flood tells the story of the rise of structural molecular biology-proteins and DNA-by immersing the reader in the original papers, written by the scientists who actually did the work. 187 pages from 42 essential scientific papers are reprinted, along with diagrams and commentaries to make them intelligible to the modern reader. The book achieves a personal note because the author was a worker in later years of the field and knew many of the key participants .

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