This extensively illustrated book by Alexander McPherson, a master practitioner, accomplishes several important goals: it presents the underlying physical and chemical principles of crystallization in an approachable way; it provides the reader with a biochemical context in which to understand and pursue successful crystal growth; it instructs the reader in practical aspects of the technologies required; and it lays out effective strategies for success that investigators can readily apply to their own experimental questions. This readable volume has been created for every investigator in biomedicine whose studies may require a shift in focus from gene to protein product, as well as chemists and physicists interested in the functions of biologically active macromolecules.

The word OC nucleation, OCO derived from OC nuclear family, OCO refers to the concept of the progenitor, or the mother and the father of any family. Only in the last few centuries have physicists OC borrowedOCO the word, and more recently, biologists for Theodor Schwann''s cell theory. Most recently, the term has come into use in atomic theory, spectroscopy, and radioactivity, as well as in the fields of atomic bombs, fission, and fusion. Nucleation as a physicochemical process is followed by two poorly understood phenomena OCo aggregation and crystallization - which underlie disorders like Alzheimer''s and OC mad-cowOCO disease (aggregation of amyloid plaque), cardiovascular diseases (deposition in coronary vessels of cholesterol and lipids), and the appearance of crystals under physiological conditions (gout, silicoses, and liver or kidney stones).Written by leading scientists in the field, including one Nobel Laureate, this book provides a unique perspective between the physical and chemical sciences on the one hand, and the biological and medical sciences on the other, and should be of considerable value to scientists, physicians, students, and the interested lay publi

For at least six hundred million years, life has been a fascinating laboratory of crystallization, referred to as biomineralization. During this huge lapse of time, many organisms from diverse phyla have developed the capability to precipitate various types of minerals, exploring distinctive pathways for building sophisticated structural architectures for different purposes. The Darwinian exploration was performed by trial and error, but the success in terms of complexity and efficiency is evident. Understanding the strategies that those organisms employ for regulating the nucleation, growth, and assembly of nanocrystals to build these sophisticated devices is an intellectual challenge and a source of inspiration in fields as diverse as materials science, nanotechnology, and biomedicine. However, “Biological Crystallization” is a broader topic that includes biomineralization, but also the laboratory crystallization of biological compounds such as macromolecules, carbohydrates, or lipids, and the synthesis and fabrication of biomimetic materials by different routes. This Special Issue collects 15 contributions ranging from biological and biomimetic crystallization of calcium carbonate, calcium phosphate, and silica-carbonate self-assembled materials to the crystallization of biological macromolecules. Special attention has been paid to the fundamental phenomena of crystallization (nucleation and growth), and the applications of the crystals in biomedicine, environment, and materials science.

Annotation Accurate molecular structures is vital for rational drug design and for structure based functional studies directed toward the development of effective therapeutic agents and drugs. Crystallography can reliably predict structure, both in terms of folding and atomic details of bonding. * Phases * Map interpretation and refinement * Analysis and software.

This edited book is written for students, postdocs and established investigators who want to enter the field of single-particle cryo-EM. This is a recently developed method to determine high-resolution structures of biological macromolecules. A major strength is the fact that cryo-EM does not require prior crystallization of protein complexes. It is especially well suited for larger complexes and molecular machines. This book, provides a comprehensive, accessible and authoritative introduction to the field. It covers all necessary background, ranging from the underlying concepts to practical aspects such as specimen preparation, data-collection, data analysis, and the final validation of results. Key features Written for students, postdocs and established investigators who want to enter the field of single-particle cryo-EM Provides a comprehensive, accessible and authoritative introduction to the field of high-resolution structure analysis by single-article cryo-EM Covers all necessary background, ranging from the underlying concepts to practical aspects such as specimen preparation, data-collection, data analysis, and the final validation of results Authors of individual sections of this book have been recruited from among the most authoritative leaders in each topic

One of the first books dedicated to the emerging field of neutron protein crystallography (NPC). It covers all of the practical aspects of NPC and demonstrates how NPC can explore protein features such as hydrogen bonds, protonation and deprotonation of amino acid residues, and hydration structures.

This unique text/reference presents an overview of the computational aspects of protein crystallization, describing how to build robotic high-throughput and crystallization analysis systems. The coverage encompasses the complete data analysis cycle, including the set-up of screens by analyzing prior crystallization trials, the classification of crystallization trial images by effective feature extraction, the analysis of crystal growth in time series images, the segmentation of crystal regions in images, the application of focal stacking methods for crystallization images, and the visualization of trials. Topics and features: describes the fundamentals of protein crystallization, and the scoring and categorization of crystallization image trials; introduces a selection of computational methods for protein crystallization screening, and the hardware and software architecture for a basic high-throughput system; presents an overview of the image features used in protein crystallization classification, and a spatio-temporal analysis of protein crystal growth; examines focal stacking techniques to avoid blurred crystallization images, and different thresholding methods for binarization or segmentation; discusses visualization methods and software for protein crystallization analysis, and reviews alternative methods to X-ray diffraction for obtaining structural information; provides an overview of the current challenges and potential future trends in protein crystallization. This interdisciplinary work serves as an essential reference on the computational and data analytics components of protein crystallization for the structural biology community, in addition to computer scientists wishing to enter the field of protein crystallization.

The precise knowledge of the structure of biological macromolecules forms the basis of understanding their function and their mechanism of action. It also lays the foundation for rational protein and drug design. The only method to obtain this knowledge is still crystallography. At present, the structures of about 400 proteins are known at or nearly at atomic proteins. However, only two of them are membrane proteins or complexes of the membrane proteins. The reasons for the difference is not the crystals of membrane proteins resists forming special problems when being analysed. The reason is that the membrane proteins resist into forming into well-ordered crystals. The intention of this book is to help to produce well-ordered crystals proteins and to provide guidelines, it is aimed at both biochemists and protein crystallographer‘s.

This book reviews current techniques used in membrane protein structural biology, with a strong focus on practical issues. The study of membrane protein structures not only provides a basic understanding of life at the molecular level but also helps in the rational and targeted design of new drugs with reduced side effects. Today, about 60% of the commercially available drugs target membrane proteins and it is estimated that nearly 30% of proteins encoded in the human genome are membrane proteins. In recent years much effort has been put towards innovative developments to overcome the numerous obstacles associated with the structure determination of membrane proteins. This book reviews a variety of recent techniques that are essential to any modern researcher in the field of membrane protein structural biology. The topics that are discussed are not commonly found in textbooks. The scope of this book includes: Expression screening using fluorescent proteins The use of detergents in membrane protein research The use of NMR Synchrotron developments in membrane protein structural biology Visualisation and X-ray data collection of microcrystals X-ray diffraction data analysis from multiple crystals Serial millisecond crystallography Serial femtosecond crystallography Membrane protein structures in drug discovery The information provided in this book should be of interest to anyone working in the area of structural biology. Students will find carefully prepared overviews of basic ideas and advanced protein scientists will find the level of detail required to apply the material directly to their day to day work. Chapters 4, 5, 6, 8 and 9 of this book are published open access under a CC BY 4.0 license at link.springer.com.