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000188456 0247_ $$2doi$$a10.1107/S1600576714010772
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000188456 1001_ $$0P:(DE-HGF)0$$aCoates, Leighton$$b0$$eCorresponding Author
000188456 245__ $$aCryogenic neutron protein crystallography: routine methods and potential benefits
000188456 260__ $$aCopenhagen$$bMunksgaard$$c2014
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000188456 520__ $$aThe use of cryocooling in neutron diffraction has been hampered by several technical challenges, such as the need for specialized equipment and techniques. This article reports the recent development and deployment of equipment and strategies that allow routine neutron data collection on cryocooled crystals using off-the-shelf components. This system has several advantages compared to a closed displex cooling system, such as fast cooling coupled with easier crystal mounting and centering. The ability to routinely collect cryogenic neutron data for analysis will significantly broaden the range of scientific questions that can be examined by neutron protein crystallography. Cryogenic neutron data collection for macromolecules has recently become available at the new Biological Diffractometer BIODIFF at the FRM II and the Macromolecular Diffractometer (MaNDi) at the Spallation Neutron Source, Oak Ridge National Laboratory. To evaluate the benefits of a cryocooled neutron structure, a full neutron data set was collected on the BIODIFF instrument on a Toho-1 [beta]-lactamase structure at 100 K.
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000188456 7001_ $$0P:(DE-HGF)0$$aTomanicek, Stephen$$b1
000188456 7001_ $$0P:(DE-Juel1)138266$$aSchrader, Tobias E.$$b2$$ufzj
000188456 7001_ $$0P:(DE-HGF)0$$aWeiss, Kevin L.$$b3
000188456 7001_ $$0P:(DE-HGF)0$$aNg, Joseph D.$$b4
000188456 7001_ $$0P:(DE-HGF)0$$aJüttner, Philipp$$b5
000188456 7001_ $$0P:(DE-HGF)0$$aOstermann, Andreas$$b6
000188456 773__ $$0PERI:(DE-600)2020879-0$$a10.1107/S1600576714010772$$gVol. 47, no. 4, p. 1431 - 1434$$n4$$p1431 - 1434$$tJournal of applied crystallography$$v47$$x1600-5767$$y2014
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