PLENARY SEMINAR March 18, 2014 10:30 AM Biology Department Auditorium Biology Building University of Puerto Rico, Mayagüez Campus Title: Biological Studies with a Free-electron X-ray Lasers Eaton Lattman, CEO Hauptman-Woodward Institute Professor Structural Biology, UB SUNY ABSTRACT: Much of what we know about the structures of protein molecules comes from the method of x-ray crystallography, in which the patterns made by x-ray beams bouncing off crystals can be transformed into three-dimensional images of molecules in the crystals themselves. The biggest bottleneck in this method is the process of growing the crystals. There is only about a 15% chance that a protein you are interested in will crystallize. The LCLS (linac coherent light source) facility at Stanford provides a new kind of x-ray beam with laser-like characteristics, and this beam will have a transformative effect on determining protein structures. • The beam is comprised of incredibly short pulses, often only 10 fempto seconds long, that are also incredibly intense. Each pulse can produce an observable pattern from a crystal that is 1000 times smaller than the ones we use today. Ultra-tiny crystals grow a lot more readily than larger ones, and so a whole universe of proteins that we could never study before will become accessible today. • The pulses in the beam act like very short flashbulbs that can freeze molecular motions, leading to the possibility of making a molecular movie that follows structural changes in the protein as it functions. • In the long-term, new generations of x-ray lasers may become so powerful that we can use the ultimate tiny crystal, a single molecule.
Posted on: Tue, 11 Mar 2014 13:28:05 +0000
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