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Protein crystallography importance

The 1980s saw many important developments in the scientific disciplines that underpin the use of protein crystallography in the pharmaceutical and biotechnology industries. Molecular biology and protein chemistry methods... [Pg.287]

Protein crystallography often requires special constructs or mutants to facilitate crystallization it also requires large quantities of highly purified protein. Thus to move forward in a timely fashion, it is important that an industrial structural biology group employ molecular biologists and individuals with expertise in protein purification. [Pg.29]

Protein-crystallography has revealed many of these groups as binding centers of heavy metals such as Pt(II), Hg(II), Au(III). It is important to note that the solution conditions in which the reagent has been applied to these crystals differ widely. If an acid pH has been used then groups with a high affinity for protons. [Pg.36]

In summary, there are three important generalizations about error estimation in protein crystallography. The first is that the level of information varies enormously as a function primarily of resolution, but also of sequence knowledge and extent of refinement. The second generalization is that no single item of information is completely immune from possible error. If the electron density map is available or indicators such as temperature factors are known from refinement, then it is possible to tell which parameters are most at risk. The third important generalization is that errors occur at a very low absolute rate 95% of the reported information is completely accurate, and it represents a detailed and objective storehouse of knowledge with which all other studies of proteins must be reconciled. [Pg.181]

The metalloproteins that have attracted most attention are those whose properties are most obviously different from those observed in the normal classical aqueous coordination chemistry of the metal ions. The challenge is to account for (initially) unique spectral or chemical properties in terms of the coordination chemistry of the metalloprotein active site, as moderated by the protein environment. With increasing frequency, as in the case of type 1 copper (Section IIIB), crystallography reveals the active site structure with sufficient clarity to provide strong clues as to the origin of the unusual spectroscopy. However, an important test of the structural and spectroscopic analyses is to reproduce the same effects in a model complex. On other occasions, as with the [4Fe-4S] proteins (Section VC), many questions remained even after the structures were known. In spite of the very impressive achievements of protein crystallography, there remain many metalloproteins for which structural data are either not available or inconclusive. [Pg.324]

Until recently, structure determination by protein crystallography was a time-consuming method accessible to a few privileged skilled practitioners. X-ray crystallography was reserved to tackle questions requiring atomic resolution details of a demonstrably important protein, often a drug target. Indeed, to... [Pg.481]

Translation function A function that can be calculated in order to determine (with respect to the unit cell axes) how a molecule, for which the orientation has been found (see Rotation function), is positioned with respect to the origin of the unit cell. This function is important in protein crystallography. [Pg.336]

There are a multitude of ways in which one can abuse this approach. Of primary importance is the quality of the pharmacological data. Inclusion of a compound with a different mechanism of action should ultimately lead to a null hypothesis, i.e. no consistent pharmacophore, but may require much effort to detect. Alternatively, the procedure may be useful in identifying compounds to be further investigated pharmacologically, similar to the use of outlayers in QSAR. One objection often raised is the obvious flexibility associated with proteins. The goal is not to compete with protein crystallography, but rather to derive a functional description of the volume available for... [Pg.219]


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