The most powerful microscopes in the world have allowed scientists to view the structures inside a cell, but they are limited in showing the details of the cell. Either the magnification is limited or the samples are not alive or working. Structural biology is the science that helps us see some of the details that are missing. It allows a view of the intricate and beautiful composition of life.

Structural biology methods dig deep below the limits and brings molecules to life in 3D and a more precise focus. It expands the limits of how a molecule works and how it functions, as well as their modifications.

It may take years, can be frustrating and tedious, but the process of determining molecular structure can be accomplished. Proteins are usually the targets for structure analysis, because they are the main active "ingredients" of the cell. They are built from a DNA template and the string of amino acids produced into very complex loops, sheets, and tangles. The structure prescribes how the protein will intermingle with other structures around the tangles in order to carry out its duties inside the cell.

The structures of molecules and the complex arrangements are breathtaking in their logic and symmetry and help scientist understand how they work. Shapes, sizes, and the construction of the molecules can be assigned to different compartments in cells and then put into context with the environment surrounding it. The main goal of structural biology is to build a model to represent cellular function.

The structure can be compared to a large city, where there are relationships formed and broken, short- or long-lived, and all are shaped or affected by the inevitable reproduction, aging, and death.

For a 3D structure of a protein it will need to be crystallized. Identical protein molecules are stabilized in a crystal lattice (mesh-like design), when blasted with X-rays, it provides diffraction data providing useful information on the spatial relationships of atoms in the protein.

With the information, the #D structure can then be built, even from scratch if necessary. However, in structural biology labs today building from scratch is not needed, comparison with other similar structures is used. The result is an artificial image of a protein structure depicting its size, how it is folded up, and overall "shape" and places where special "decorations" are attached. The real protein structure in nature is more dynamic and indistinct.

There are proteins which may be hard to crystallize, and other techniques are then used to determine structure. Other methods include nuclear magnetic resonance, microscopy, electron tomography or mass spectroscopy and give different views of proteins at different scales.

All the techniques may also be brought together to get the most effective and most accurate structure of a protein. In addition, the structure gives more information than just the space it fills. Correlating information from the many techniques into one structure and telling how the protein works, where it fits inside or outside the cell, and the other interacting molecules is called correlative structural biology.

The cell landscape can then be used to identify proteins or even specific parts of proteins that can be targets of designer drugs, modify behavior of or disable a dysfunctional protein. Structural biology brings unique information to programs related to drug or vaccine discovery.

It is the significant basis for modern strategies to improve health for the future.

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