A new crystallographic technique developed at the University of Leeds is set to transform scientists' ability to observe how molecules work. A research paper, published online in the journal Nature Methods on October 5, 2014, describes a new way of doing time-resolved crystallography, a method that researchers use to observe changes within the structure of molecules. The article is entitled, “Time-Resolved Crystallography Using the Hadamard Transform.” Although fast time-resolved crystallography (Laue crystallography) has previously been possible, it has required advanced instrumentation that is only available at three sites worldwide. Only a handful of proteins have been studied using the traditional technique. The new method will allow researchers across the world to carry out dynamic crystallography and is likely to provide a major boost in areas of research that rely on understanding how molecules work, such as the development of novel smart materials or new drugs. Observing how structure and dynamics are linked to function is key to designing better medicines that are targeted at specific states of molecules, helping to avoid unwanted side effects. "A time-resolved structure is a bit like having a movie for crystallographers," said Professor Arwen Pearson, who led the team at Leeds. "Life wiggles. It moves about and, to understand it, you need to be able to see how biological structures move at the atomic scale. This breakthrough allows us to do that." Traditional X-ray crystallography fires X-rays into crystallized molecules and creates an image that allows researchers to work out the atomic structure of the molecules. A major limitation is that the picture created is the average of all the molecules in a crystal and their motions over the time of an experiment. Dr.
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