This important book presents a comprehensive account of the techniques & applications of single crystal neutron diffraction in the area of chemical crystallography & molecular structure. Beginning with a brief description of the general principles & the reasons for choosing the technique - the "why" - the book covers the methods for both the production of neutrons & the measurement of their scattering by molecular crystals - the "how" - followed by a detailed survey of past, present & future applications - the "what". The coverage of both steady state & pulsed neutron sources & instrumentation is extensive, while the survey of applications is the most comprehensive yet undertaken. The book endeavours to show why the technique is an essential method for studying areas as diverse as hydrogen bonding & weak interactions, organometallics, supramolecular chemistry & crystal engineering, metal hydrides, charge density & pharmaceuticals. It is an ideal reference source for the research worker interested in using neutron diffraction to study the structure of molecules. Contents: Crystallography & the Importance of Structural Information; Neutron Scattering; Neutron Diffractometers; Review of Applications I: The Accurate Location of Atoms; Review of Applications II: Hydrogen Bonding & Other Intermolecular Interactions; Review of Applications III: Probing Vibrations & Disorder; Impact on Material Properties & Design; The Future: New Instruments, New Sources, New Techniques. Readership: Students & researchers involved in structural science, especially chemical crystallography.

This book aims to explain how and why the detailed three-dimensional architecture of molecules can be determined by an analysis of the diffraction patterns obtained when X rays or neutrons are scattered by the atoms in single crystals. Part 1 deals with the nature of the crystalline state, diffraction generally, and diffraction by crystals in particular, and, briefly, the experimental procedures that are used. Part II examines the problem of converting the experimentally obtained data into a model of the atomic arrangement that scattered these beams. Part III is concerned with the techniques for refining the approximate structure to the degree warranted by the experimental data. It also describes the many types of information that can be learned by modern crystal structure analysis. There is a glossary of terms used and several appendixes to which most of the mathematical details have been relegated.

Detennination of the magnetic structure of magnetic materials is a fundamental problem that can be solved by magnetic neutron diffraction techniques. By magnetic structures we refer to the mutual alignment of the magnetic moments of the atoms in a crystal and their overall alignment relative to the crystallographic axes. Some indirect, tentative data on the magnetic structure of magnetic materials can be obtained from research on their magnetic, mechanical, thermal, and other properties. But only neutron diffraction is a unique direct method of detennining the magnetic structure of a crystal. The magnetic structure of more than one thousand crystals with magnetic order has been studied during 30 years of neutron diffraction research made on reactors in a large number of laboratories in the world. The results of this research work are extensively described in the handbook Magnetic Structures Determined by Neutron Diffraction [176]; in the present book, we will often refer to this handbook. The first extensive theoretical generalization of the principles of magnetic neutron diffraction and the results of research on magnetic structures appeared in the book by Yu. A. Izyumov and R. P. Ozerov Magnetic Neutron Diffraction [24, 134].

The inter action between the magnetic field generated by the neutron and the magnetic moment of atoms containing unpaired electrons was experimentally demonstrated for the first time about twenty years ago. The basic theory describing such an in teraction had already been developed and the first nuclear reactors with large available thermal neutron fluxes had recently been con structed. The power of the magnetic neutron interaction for in vestigating the structure of magnetic materials was immediately recognized and put to use where possible. Neutron diffraction, however, was practicable only in countries with nuclear reactors. The earliest neutron determinations of magnetic ordering were hence primarily carried out at Oak Ridge and Brookhaven in the US, at Chalk River in Canada and at Harwell in England. Diffraction patterns from polycrystalline ferromagnets and antiferromagnets are interpretable if produced by simple spin arrays. More complex magnetic scattering patterns could often be unravelled, in terms of a three-dimensional array of atomic moments, if the specimen studied is a single crystal. The devel opment of sophisticated cryogenic equipment, with independently alignable magnetic fields, opened the way to greater complexity in the magnetic structures that could be successfully determined, as did also the introduction of polarized neutron beams. By the end of the 'sixties, many countries were contributing significantly to neutron diffraction studies of a wide variety of magnetic materials.

Crystallography may be described as the science of the structure of materi als, using this word in its widest sense, and its ramifications are apparent over a broad front of current scientific endeavor. It is not surprising, therefore, to find that most universities offer some aspects of crystallography in their undergraduate courses in the physical sciences. It is the principal aim of this book to present an introduction to structure determination by X-ray crystal lography that is appropriate mainly to both final-year undergraduate studies in crystallography, chemistry, and chemical physics, and introductory post graduate work in this area of crystallography. We believe that the book will be of interest in other disciplines, such as physics, metallurgy, biochemistry, and geology, where crystallography has an important part to play. In the space of one book, it is not possible either to cover all aspects of crystallography or to treat all the subject matter completely rigorously. In particular, certain mathematical results are assumed in order that their applications may be discussed. At the end of each chapter, a short bibliog raphy is given, which may be used to extend the scope of the treatment given here. In addition, reference is made in the text to specific sources of information. We have chosen not to discuss experimental methods extensively, as we consider that this aspect of crystallography is best learned through practical experience, but an attempt has been made to simulate the interpretive side of experimental crystallography in both examples and exercises.

This book provides a comprehensive and up-to-date introduction to the fundamental theory and applications of slow-neutron scattering.

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