Biological molecules are the machinery of life. Each year hundreds of scientists come to SLAC's Stanford Synchrotron Radiation Lightsource (SSRL) to investigate the structures of molecules such as proteins, viruses and nucleic acids. Protein crystallography, the primary technique used to study the building blocks that make up living organisms, is one of the most active areas of research at SLAC.
To determine the structure of a biological molecule, scientists first grow the molecule into a crystal usually no bigger than a grain of salt, in which all the atoms are ordered into a regular pattern. The crystallized sample is then exposed to a thin beam of intense, highly focused X-rays created by SSRL's synchrotron accelerator. The X-rays are "scattered" by the atoms into a unique pattern of spots on a detector, and the spots are used to work out the structure of the molecules atom by atom.
This technique earned Stanford University’s Roger Kornberg the 2006 Nobel Prize in Chemistry. Kornberg and colleagues used protein crystallography to solve the structure of RNA polymerase, which contains over 30,000 individual atoms. RNA polymerase plays a key role in how information stored in DNA is translated into the proteins of life.
Starting in 2009, the Linac Coherent Light Source at SLAC stands to revolutionize protein crystallography by making "single shot" images of molecules that resist forming crystals.
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