Buch, Englisch, 332 Seiten, Previously published in hardcover, Format (B × H): 155 mm x 235 mm, Gewicht: 528 g
Buch, Englisch, 332 Seiten, Previously published in hardcover, Format (B × H): 155 mm x 235 mm, Gewicht: 528 g
ISBN: 978-1-4419-2210-6
Verlag: Springer
X-ray crystallography is an established method for studying the structure of proteins and other macromolecules. As the importance of proteins grows, researchers in many fields have found that a working knowledge of X-ray diffraction is an indispensable tool. In this new edition of his essential work, Dr. Jan Drenth, recognized internationally for his numerous contributions to crystallographic research, provides an up-to-date and technically rigorous introduction to the subject. Principles of Protein X-ray Crystallography provides the theoretical background necessary to understand how the structure of proteins is determined at atomic resolution. The book is an introduction for graduate students, postdoctoral researchers, and established scientists who want to use protein crystallography in their own endeavors, or need to understand the subject in order to critically evaluate the literature. New material in the 3rd edition includes a section on twinning, an additional chapter on crystal growth and a discussion of single-wavelength anomalous dispersion.
Zielgruppe
Graduate
Autoren/Hrsg.
Fachgebiete
- Naturwissenschaften Biowissenschaften Angewandte Biologie Biophysik
- Naturwissenschaften Biowissenschaften Proteinforschung
- Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
- Naturwissenschaften Chemie Analytische Chemie
- Naturwissenschaften Chemie Physikalische Chemie Chemische Kristallographie
- Naturwissenschaften Physik Angewandte Physik Biophysik
Weitere Infos & Material
Crystallizing a Protein.- X-ray Sources and Detectors.- Crystals.- Theory of X-ray Diffraction by a Crystal.- Average Reflection Intensity and Distribution of Structure Factor Data.- Special Forms of the Structure Factor.- The Solution of the Phase Problem by the Isomorphous Replacement Method.- Phase Improvement.- Anomalous Scattering in the Determination of the Protein Phase Angles and the Absolute Configuration.- Molecular Replacement.- Direct Methods.- Laue Diffraction.- Refinement of the Model Structure.- The Combination of Phase Information.- Checking for Gross Errors and Estimating the Accuracy of the Structural Model.- Practical Protein Crystallization.