Crystallographic Methods and Protocols by Mark R. Sanderson (auth.), Christopher Jones, Barbara

By Mark R. Sanderson (auth.), Christopher Jones, Barbara Mulloy, Mark R. Sanderson (eds.)

In Crystallographic tools and Protocols top experts within the software of X-ray crystallography to organic difficulties offer a easy and accomplished advisor to its profitable use in acquiring exact third-dimensional constructions of proteins, nucleic acids, and their complexes. those deeply skilled researchers describe in transparent sensible phrases their confirmed tools for getting ready samples, crystallizing them, acquiring initial characterizations, buying and interpreting facts, and fixing and refining buildings. Their step by step directions provide biologically expert staff speedy entry to a strong approach necessary to fixing many biologically proper difficulties.

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Affinity chromatography provides high specificity by exploiting the biological properties of the molecule, which is reversibly adsorbed to an immobilized ligand coupled to an insoluble matrix. Some applications of affinity chromatography are given in Table 2. , cyanogen bromide-activated Sepharose (Pharmacia-Biotech). Immunoadsorbants offer high binding capacities and extremely high specificity, but the method used for desorption or elution is critical. Sometimes such harsh conditions are required that the protein becomes irreversibly denatured.

Danvers, MA). , polyethylene glycol (PEG), may be employed as an initial fractionation step. Conditions of high protein concentration, low temperatures, and pH close to neutrality are generally used in salt fractionation. Ammonium sulfate is the most commonly used salt, chiefly because of its high solubility and stabilizing properties. A nomogram and various charts have been devised (43) for determining the amount of salt to be added to the protein fraction to attain the required saturation. , plasma proteins, histones, and polypeptide hormones, but are not to be recommended for unstable proteins.

Oxford University Press, New York. , Podjarny, A. , and Thierry, 1. C. ) (1991) Crystallographic Computing 5. Oxford University Press, New York. ) Rollett, J. S. (1965) Computing Methods in Crystallography. Pergamon Press, Oxford. Rossman, M. G. ) (1972) The Molecular Replacement Method. Gordon and Breach, New York. Wyckoff, H. , Hirs, C. H. , and Timasheff, S. N. ) (1985) Diffraction Methodsfor Biological Macromolecules. Methods in Enzymology, vols. 114 and 115. Academic, New York. CCP4 Weekend Workshops The contributions to these workshops (which are organized by the CCP4 workgroup) are written up and circulated to the participants.

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