Purification and demonstration of purity were the primary reasons that techniques were developed for the crystallization of naturally occurring proteins in the laboratory. Protein crystallization was marked by major successes throughout the s and s, with the crystallization of insulin Abel et al. In the s Northrop and coworkers purified a number of important enzymes by crystallization, most notably from the pancreas of pigs and cows reviewed in Northrop et al. A cascade of successes with other enzymes quickly followed, leading to the award of Nobel Prizes to Sumner and Northrop. The early work of Bernal, Fankuchen, Crowfoot and Perutz Dickerson, made protein crystals important for the three-dimensional structural information that they could potentially yield. The demand for protein crystals expanded rapidly in the s and s as protein crystallography came of age and highly motivated young scientists entered the field.
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The History and Character of Macromolecular Crystals -- 2. The Purification and Characterization of Biological Macromolecules -- 4. Some Physical and Energetic Principles -- 5. Practical Procedures for Macromolecular Crystallization -- 6.
Important Considerations in Macromolecular Crystallization -- 7. Strategies and Special Approaches in Growing Crystals -- 8. Impurities, Defects, and Crystal Quality -- 9. Crystal Growth in Unique Environments. Responsibility: A. Abstract: 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.
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The History and Character of Macromolecular Crystals -- 2. The Purification and Characterization of Biological Macromolecules -- 4. Some Physical and Energetic Principles -- 5. Practical Procedures for Macromolecular Crystallization -- 6. Important Considerations in Macromolecular Crystallization -- 7. Strategies and Special Approaches in Growing Crystals -- 8. Impurities, Defects, and Crystal Quality -- 9.
Crystallization of biological macromolecules
McPherson and B. Cudney For the successful X-ray structure determination of macromolecules, it is first necessary to identify, usually by matrix screening, conditions that yield some sort of crystals. Initial crystals are frequently microcrystals or clusters, and often have unfavorable morphologies or yield poor diffraction intensities. It is therefore generally necessary to improve upon these initial conditions in order to obtain better crystals of sufficient quality for X-ray data collection. Even when the initial samples are suitable, often marginally, refinement of conditions is recommended in order to obtain the highest quality crystals that can be grown. The quality of an X-ray structure determination is directly correlated with the size and the perfection of the crystalline samples; thus, refinement of conditions should always be a primary component of crystal growth. The improvement process is referred to as optimization, and it entails sequential, incremental changes in the chemical parameters that influence crystallization, such as pH, ionic strength and precipitant concentration, as well as physical parameters such as temperature, sample volume and overall methodology.