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The structure of the Mre11 protein bound to DNA
Date:10/3/2008

lped develop and is in charge of the MX facility, and Greg Hura, also of PBD, helped develop and is in charge of the SAXS facility. The Scripps Institute's Williams was sometimes able to work by remote control from La Jolla using the advanced automation at the SIBYLS end station, whose robots and software can load samples, track ongoing experiments in real time, and collect data.

"Some difficult-to-crystallize macromolecular complexes can result in large unit cells that are hard to work with. The MX endstation of SIBYLS is designed to address these challenges, for example with a large-area detector that can be positioned very far from the sample," says Classen. "While crystallography can give you nice pictures of static molecules, however, it isn't as informative when it comes to dynamic processes. That's where SAXS comes in; it's a perfect complement to MX."

Says Hura, "SAXS is a solution-imaging technique, where each experiment measures the sum of all conformations of the molecule. While the ultimate resolution of crystallography is higher, SAXS may be used to determine the flexibility of proteins as they perform their functions and it can resolve the ambiguities of crystallography by showing what possible structures are the most likely."

Tainer, leader of SIBYLS, says "You get information from every protein crystal you analyze if only what not to try crystallizing. Sometimes you can only crystallize a small part of a large protein or complex. It's the synergy with SAXS, which can show you how these pieces fit together or provide experimental evidence for the best among competing models, that makes this beamline combining both techniques so very valuable to the missions of both NCI and DOE."


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Contact: Paul Preuss
paul_preuss@lbl.gov
510-486-6249
DOE/Lawrence Berkeley National Laboratory
Source:Eurekalert  

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