Cryogenic Neutron Protein Crystallography: routine methods and potential benefits

Journal Article · Fri Aug 01 00:00:00 EDT 2014 · Journal of Applied Crystallography

DOI:https://doi.org/10.1107/S1600576714010772· OSTI ID:1156718

Weiss, Kevin L.  ^[1]; Tomanicek, Stephen J. ^[1]; NG, Joseph D. ^[1]

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1. ORNL

The use of cryocooling in neutron diffraction has been hampered by several technical challenges such as the need for specialized equipment and techniques. Recently we have developed and deployed equipment and strategies that allow for 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 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 we collected a full neutron data set on the BIODIFF instrument on a Toho-1 lactamase structure at 100K.

• Research Organization: Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC05-00OR22725
• OSTI ID: 1156718
• Journal Information: Journal of Applied Crystallography, Vol. 47, Issue n/a
• Country of Publication: United States
• Language: English