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X-ray crystallography can provide very detailed atomic information, showing every atom in a protein or nucleic acid along with atomic details of ligands, inhibitors, ions, and other molecules that are incorporated into the crystal. However, the process of crystallization is difficult and can impose limitations on the types of proteins that may be studied by this method. For example, X-ray crystallography is an excellent method for determining the structures of rigid proteins that form nice, ordered crystals. Flexible proteins, on the other hand, are far more difficult to study by this method because crystallography relies on having many, many molecules aligned in exactly the same orientation, like a repeated pattern in wallpaper. Flexible portions of protein will often be invisible in crystallographic electron density maps, since their electron density will be smeared over a large space. This is described in more detail on the page about Womens Pure Beauty Briefs Sans Complexe Clearance Wide Range Of Discount Manchester Outlet In China Cheap Sast mdGmDLQ
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New technology, termed serial femtosecond crystallography, is revolutionizing the methods of X-ray crystallography. A free electron X-ray laser (XFEL) is used to create pulses of radiation that are extremely short (lasting only femtoseconds) and extremely bright. A stream of tiny crystals (nanometers to micrometers in size) is passed through the beam, and each X-ray pulse produces a diffraction pattern from a crystal, often burning it up in the process. A full data set is compiled from as many as tens of thousands of these individual diffraction patterns. The method is very powerful because it allows scientists to study molecular processes that occur over very short time scales, such as the absorption of light by biological chromophores.

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