Furthermore, most of the therapeutically active compounds target proteins and thus structural knowledge is indispensable for revealing relevant drug–protein interactions to improve existing or design novel drugs. The molecular structure of proteins determines their properties and functions, which is of tremendous interest to scientists working in many areas of life sciences as proteins are involved in the most basic processes of life. Structural biology is concerned with the molecular structure and dynamics of biological macromolecules, particularly proteins and nucleic acids. In this lecture text, the development of POMs as tools in protein crystallography are discussed with a special focus on the so far most successful cluster TEW. In this regard, the tellurium-centered Anderson–Evans polyoxotungstate 6− (TEW) showed its high potential as crystallization additive. In recent years, polyoxometalates (POMs) emerged as a promising group of crystallization additives due to their unique structures and properties. Therefore, a more universal additive addressing a wider range of proteins and being applicable to a broad spectrum of crystallization conditions would represent a significant advance in the field of protein crystallography. Most of the commonly used additives are, however, restricted to particular crystallization conditions or groups of proteins. Many strategies have been developed in the past decades to improve or enable the crystallization of proteins, whereby the use of so-called additives, which are mostly small molecules that make proteins more amenable to crystallization, is one of the most convenient and successful methods. Crystallization is still more or less a ‘trial and error’ based procedure, and therefore, very time and resource consuming. However, protein crystallography suffers from some major drawbacks, whereby the unpredictability of the crystallization process represents the main bottleneck. As the structure determines the functions and properties of a protein, crystallography is of immense importance for nearly all research fields related to biochemistry. Portable WAXS set up with sample autolader.Protein crystallography is the most widely used method for determining the molecular structure of proteins and obtaining structural information on protein–ligand complexes at the atomic level. Fischetti et al, The BioCAT undulator beamline 18ID: a facility for biological non‐crystalline diffraction and X‐ray absorption spectroscopy at the Advanced Photon Source (2004) J. Since every crystal solid as its unique pattern of d-spacing (powder pattern), the chemical characteristics can be determined.įigure 1. The intensity of the d-spacing is proportional to the number of electrons/atoms in the structure. The distance between the imaginary planes is called d-spacing. A crystalline solid can consist of regularly spaced atoms (electrons) that are referred as imaginary planes. When X-rays are directed at the solids, they are scattered in some certain patterns depend on the internal structure of the material. For SAXS, it covers much smaller angle, which is up to 1 degree. The scattering intensity is plotted as a function of the 2θ angle. X-rays are scattered by the electrons in a material. A goniometer is an instrument that either measures the angles or allows an object to be rotated to a precise angle. The sample is scanned in a wide-angle X-ray goniometer.
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