Eaton E. Lattman

Dynamics and Kinetics in Structural Biology Understand the latest experimental tools in structural biology with this pioneering work Structural biology seeks to understand the chemical mechanisms and functions of biological molecules, such as proteins, based on their atomic structures. Until recently, these structures have been studied only statically, using procedures which deliberately freeze atomic motion. However, freezing eliminates the rapid structural motions so essential to biological activity and function; the molecules are inactive. But with the recent development of X-ray free electron laser (XFEL) sources, efforts to conduct dynamic experiments have expanded using the principles of dynamics and kinetics to capture active biological molecules as they function. Dynamics and Kinetics in Structural Biology promotes the development of these experiments and their successful application. It grounds readers in the foundational principles of dynamics and kinetics; proceeds through extended discussions of experimental procedures and data analysis techniques; and explores experimental frontiers in structural dynamics. The book will aid researchers to gather and interpret cutting-edge data on the dynamic structure of biological molecules, under conditions where they retain their biological functions. Dynamics and Kinetics in Structural Biology offers readers: Authorship by founding figures in the fieldIn-depth presentation of time-resolved X-ray crystallography, solution scattering, and moreA pioneering contribution to a rapidly developing field of study Dynamics and Kinetics in Structural Biology is essential reading for graduate students, scientists, researchers and industry professionals engaged in structural studies of biological systems. Industry professionals considering dynamic studies in the development of new product lines will also benefit.

Small angle solution scattering (SAS) is increasingly being applied to biological problems. It is a complementary technique that, when applied in appropriate circumstances with carefully structured questions, can provide unique information not available from other techniques. While small angle solution scattering has been around for some time, a confluence of recent developments has dramatically enhanced its power. Intense third generation X-ray sources, low noise detectors, development of new algorithms and the computational power to take advantage of these have all matured, and use of free-electron x-ray laser sources is on the horizon. Whole new classes of experiments and analyses have been created as a result. These include the generation of molecular envelopes, the ability to do time-resolved studies, and the ability to account for structural changes using modelling based on the SAS data. The technical improvements have also reduced the amount of time and material needed to carry out an experiment. Beamtime at synchrotron sources is in demand, workshops on the subject are popular and researchers adopting the technique as part of their repertoire are growing. With these in mind, this book was written to guide structural biologists who may wish to adopt the technique, understand its strengths and weaknesses or just have a general interest in its potential.

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.

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.