scholarly journals Neutron protein crystallography at the Heinz Maier-Leibnitz Zentrum (MLZ): new developments and recent application examples

2019 ◽  
Vol 75 (a2) ◽  
pp. e134-e134
Author(s):  
Tobias E. Schrader ◽  
Andreas Ostermann ◽  
Michael Monkenbusch ◽  
Bernhard Laatsch ◽  
Philipp Jüttner ◽  
...  
Keyword(s):  
Protein Crystallography ◽  
Recent Application ◽  
New Developments ◽  
Neutron Protein Crystallography

scholarly journals Neutron protein crystallography at the Heinz Meier-Leibnitz Zentrum (MLZ): new developments and recent application examples

2018 ◽  
Vol 74 (a2) ◽  
pp. e177-e177
Author(s):  
Tobias Erich Schrader ◽  
Andreas Ostermann ◽  
Michael Monkenbusch ◽  
Bernhard Laatsch ◽  
Philipp Jüttner ◽  
...  
Keyword(s):  
Protein Crystallography ◽  
Recent Application ◽  
New Developments ◽  
Neutron Protein Crystallography

scholarly journals Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography

2010 ◽  
Vol 66 (11) ◽  
pp. 1144-1152 ◽  
Author(s):  
Andrey Kovalevsky ◽  
Toshiyuki Chatake ◽  
Naoya Shibayama ◽  
Sam-Yong Park ◽  
Takuya Ishikawa ◽  
...  
Keyword(s):  
Protein Crystallography ◽  
Human Adult ◽  
Normal Human ◽  
Adult Hemoglobin ◽  
Neutron Protein Crystallography ◽  
Key Residues

Cryogenic neutron protein crystallography: routine methods and potential benefits

2014 ◽  
Vol 47 (4) ◽  
pp. 1431-1434 ◽  
Author(s):  
Leighton Coates ◽  
Stephen Tomanicek ◽  
Tobias E. Schrader ◽  
Kevin L. Weiss ◽  
Joseph D. Ng ◽  
...  
Keyword(s):  
Data Collection ◽  
Cooling System ◽  
National Laboratory ◽  
Protein Crystallography ◽  
Neutron Data ◽  
Data Set ◽  
Oak Ridge ◽  
Specialized Equipment ◽  
Potential Benefits ◽  
Neutron Protein Crystallography

The 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 β-lactamase structure at 100 K.

Neutron protein crystallography reveals unique details of clinical drug binding to a human target enzyme

Neutron News ◽  
2013 ◽  
Vol 24 (4) ◽  
pp. 20-23
Author(s):  
Mayank Aggarwal ◽  
Andrey Kovalevsky ◽  
Robert McKenna ◽  
David Silverman ◽  
Zoë Fisher
Keyword(s):  
Protein Crystallography ◽  
Drug Binding ◽  
Neutron Protein Crystallography ◽  
Clinical Drug ◽  
Target Enzyme
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